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1.
Plant immunity frequently involves the recognition of pathogen-encoded avirulence (avr) factors by their corresponding plant resistance (R) proteins. This triggers the hypersensitive response (HR) where necrotic lesions formed at the site(s) of infection help restrict pathogen spread. HRT is an Arabidopsis R protein required for resistance to turnip crinkle virus (TCV). In a genetic screen for mutants compromised in the recognition of TCV's avr factor, we identified crt1 (compromised recognition of TCV), a mutant that prematurely terminates an ATPase protein. Following TCV infection, crt1 developed a spreading HR and failed to control viral replication and spread. crt1 also suppressed HR-like cell death induced by ssi4, a constitutively active R protein, and by Pseudomonas syringae carrying avrRpt2. Furthermore, CRT1 interacts with HRT, SSI4, and two other R proteins, RPS2 and Rx. These data identify CRT1 as an important mediator of defense signaling triggered by distinct classes of R proteins. 相似文献
2.
Resistance (R) gene-mediated immunity provides plants with rapid and strain-specific protection against pathogen infection. Our recent study using the genetically tractable Arabidopsis and turnip crinkle virus (TCV) pathosystem revealed a novel component, named CRT1 (compromised for recognition of the TCV CP), that is involved in general R gene-mediated signaling, including that mediated by HRT, an R gene against TCV. The Arabidopsis CRT1 gene family contains six additional members, of which two share high homology to CRT1 (75 and 81% a.a. identity); either CRT1 or its closest homolog restore the cell death phenotype suppressed by crt1. Analysis of single knock-out mutants for CRT1 and its closest homologs suggest that each may have unique and redundant functions. Here, we provide insight into the screening conditions that enabled identification of a mutant gene despite the presence of functionally redundant family members. We also discuss a potential mechanism that may regulate the interaction between CRT1 and R proteins.Key words: resistance gene, ATPase, suppressor screening, Arabidopsis, turnip crinkle virusPlant resistance (R) proteins activate defense signaling pathways following detection of a specific pathogen-encoded effector, or perception that a host factor has been altered by a pathogen effector. The vast majority of R proteins contain nucleotide binding site (NBS) and leucine-rich repeat (LRR) domains. These R proteins can be further divided into two subgroups, TIR-NBS-LRR and CC-NBS-LRR, depending on whether the N terminus consists of a Toll-interleukin 1 receptor (TIR) or a coiled-coiled (CC) domain, respectively.1 Subsequent to pathogen perception, the signal(s) generated by various R proteins likely converge into a limited set of pathways, with CC-NBS-LRR proteins usually utilizing NDR1 and TIR-NBS-LRR proteins generally requiring EDS1.2 However, the molecular mechanism(s) through which R proteins recognize a pathogen(s) and initiate a defense signal(s) remains unclear.To gain insights into this elusive signaling process, several groups have performed genetic screens to isolate mutants whose R gene-mediated resistance responses are suppressed following either pathogen infection or expression of a transgene-encoded bacterial effector protein. Several proteins, including HSP90, SGT1 and RAR1, were shown to be required for resistance triggered by a variety of R proteins, suggesting their universal function in R protein-mediated resistance.3–7 However, while some R protein-mediated signaling pathways required both RAR1 and SGT1, others needed only one or neither protein. Thus, the requirement for RAR1 and SGT1 appears to be specific to each pathway.8 Further studies revealed that SGT1, RAR1 and HSP90 regulate the stability/accumulation of various R proteins,8–11 raising the possibility that they serve as (co)chaperones for assembling an active R protein complex.The Arabidopsis R protein HRT was previously shown to recognize the coat protein (CP) of turnip crinkle virus (TCV) and trigger necrotic lesion formation in the inoculated leaf, as well as local and systemic defense responses.12 To identify components of the HRT-mediated signaling pathway, a line containing HRT and an inducible CP transgene was constructed and screened for suppressors of CP-induced cell death.13 One mutant, named crt1 (compromised for recognition of the TCV CP), was identified; it contains a mutation in a GHKL (Gyrase, Hsp90, histidine kinase, MutL) ATPase.13 Interestingly, HSP90 also belongs to this recently recognized ATPase superfamily, although sequence homology between HSP90 and CRT1 is limited to the ATPase domain.14 Either wt CRT1 or its closest homolog, CRT1-h1 (81% a.a. identity to CRT1; 13 suggesting that CRT1 and CRT1-h1 are functionally redundant.
Open in a separate windowGiven the presence of a functionally redundant homolog sharing 81% a.a. identity to CRT1, it is surprising that the crt1 mutant was identified. Because a previous study using the dexamethasone inducible system reported severe growth arrest and induction of defense-related genes when any transgene was highly expressed,15 we started with a transgenic line expressing CP at a level that was low (particularly in comparison to those attained during TCV infection), yet was sufficient to trigger cell death in non-mutant plants. The low level of CP expression in our transgenic line may have inadvertently provided screening conditions under which a rather modest compromise in R protein-mediated signaling could be detected, such as a mutation in a gene with functionally redundant family members. The crt1 and other crt mutants indeed showed cell death when CP was highly expressed via TCV infection. Thus, it is likely that crt1 would have escaped the suppressor screen if expression of the CP transgene had been higher. Another anti-viral R protein of Arabidopsis, RCY1, was utilized for a similar suppressor screen except that the effector protein was provided via viral infection.16 This screen identified mutations only in RCY1, consistent with our hypothesis that weak activation of the defense signaling pathway facilitated detection of a mutation in a gene that is part of a functionally redundant family.Since HRT-mediated resistance to TCV was impaired in crt1 and was further compromised by silencing closely related CRT1 family members,13 the functional copy number of CRT1 family members appears to be important for resistance. This result, combined with the semi-dominant nature of the crt1 mutation led us to test whether the mutant phenotype is due to haploid insufficiency. Analysis of single T-DNA knockout mutants for CRT1 or CRT1-h1 revealed that resistance to Pseudomonas syringae was not compromised, although it was suppressed in a double knockout mutant (unpublished). These results suggest that loss of a single copy of CRT1 is not sufficient to compromise TCV resistance signaling, thereby arguing that the crt1 phenotype is due to a dosage effect of disabled CRT1 family members. An alternative, although mutually not exclusive, possibility is that crt1 suppresses TCV resistance via a negative gain of function. Ectopic expression of some truncated CRT1 variants suppressed cell death triggered by the constitutively activated R protein ssi4.13 Thus, crt1 might suppress resistance signaling by competing with wild type CRT1 for an interacting partner, likely an R protein. Such a scenario could explain why CRT1 dosage affects TCV resistance.An intriguing possibility raised in a preview to our paper is that CRT1 may activate/prime a cytosolic R protein, which is then localized to the nucleus.17 Several lines of evidence suggest that nuclear localization of some R proteins is required for their function.18–20 Thus, CRT1 could be an important player that transits R proteins from one subcellular location to another, although it remains to be demonstrated whether HRT and the other R proteins shown to interact with CRT1 change subcellular location during resistance signaling. Another important question is what triggers CRT1 to activate/prime a client R protein. Western analysis has revealed that CRT1 is present as two distinct isoforms; the larger isoform presumably is created by an unknown post-translational modification.13 Interestingly, the larger CRT1 isoform interacts poorly with the NBS domain of HRT,13 suggesting that this putative modification is a crucial signal to release a client R protein. Thus, characterization of this post-translational modification may provide crucial insight into an R protein-mediate signaling pathway(s) that has been enigmatic for over a decade. 相似文献
Table 1
Amino-acid sequence identity between CRTI family members in ArabidopsisOpen in a separate window |
3.
An EDS1 orthologue is required for N-mediated resistance against tobacco mosaic virus 总被引:12,自引:0,他引:12
Peart JR Cook G Feys BJ Parker JE Baulcombe DC 《The Plant journal : for cell and molecular biology》2002,29(5):569-579
In Arabidopsis, EDS1 is essential for disease resistance conferred by a structural subset of resistance (R) proteins containing a nucleotide-binding site, leucine-rich-repeats and amino-terminal similarity to animal Toll and Interleukin-1 (so-called TIR-NBS-LRR proteins). EDS1 is not required by NBS-LRR proteins that possess an amino-terminal coiled-coil motif (CC-NBS-LRR proteins). Using virus-induced gene silencing (VIGS) of a Nicotiana benthaminana EDS1 orthologue, we investigated the role of EDS1 in resistance specified by structurally distinct R genes in transgenic N. benthamiana. Resistance against tobacco mosaic virus mediated by tobacco N, a TIR-NBS-LRR protein, was EDS1-dependent. Two other R proteins, Pto (a protein kinase), and Rx (a CC-NBS-LRR protein) recognizing, respectively, a bacterial and viral pathogen did not require EDS1. These data, together with the finding that expression of N. benthamiana and Arabidopsis EDS1 mRNAs are similarly regulated, lead us to conclude that recruitment of EDS1 by TIR-NBS-LRR proteins is evolutionarily conserved between dicotyledenous plant species in resistance against bacterial, oomycete and viral pathogens. We further demonstrate that VIGS is a useful approach to dissect resistance signaling pathways in a genetically intractable plant species. 相似文献
4.
Role of SGT1 in resistance protein accumulation in plant immunity 总被引:20,自引:0,他引:20
Azevedo C Betsuyaku S Peart J Takahashi A Noël L Sadanandom A Casais C Parker J Shirasu K 《The EMBO journal》2006,25(9):2007-2016
A highly conserved eukaryotic protein SGT1 binds specifically to the molecular chaperone, HSP90. In plants, SGT1 positively regulates disease resistance conferred by many Resistance (R) proteins and developmental responses to the phytohormone, auxin. We show that silencing of SGT1 in Nicotiana benthamiana causes a reduction in steady-state levels of the R protein, Rx. These data support a role of SGT1 in R protein accumulation, possibly at the level of complex assembly. In Arabidopsis, two SGT1 proteins, AtSGT1a and AtSGT1b, are functionally redundant early in development. AtSGT1a and AtSGT1b are induced in leaves upon infection and either protein can function in resistance once a certain level is attained, depending on the R protein tested. In unchallenged tissues, steady-state AtSGT1b levels are at least four times greater than AtSGT1a. While the respective tetratricopeptide repeat (TPR) domains of SGT1a and SGT1b control protein accumulation, they are dispensable for intrinsic functions of SGT1 in resistance and auxin responses. 相似文献
5.
Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation 总被引:12,自引:0,他引:12
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Tameling WI Vossen JH Albrecht M Lengauer T Berden JA Haring MA Cornelissen BJ Takken FL 《Plant physiology》2006,140(4):1233-1245
Resistance (R) proteins in plants confer specificity to the innate immune system. Most R proteins have a centrally located NB-ARC (nucleotide-binding adaptor shared by APAF-1, R proteins, and CED-4) domain. For two tomato (Lycopersicon esculentum) R proteins, I-2 and Mi-1, we have previously shown that this domain acts as an ATPase module that can hydrolyze ATP in vitro. To investigate the role of nucleotide binding and hydrolysis for the function of I-2 in planta, specific mutations were introduced in conserved motifs of the NB-ARC domain. Two mutations resulted in autoactivating proteins that induce a pathogen-independent hypersensitive response upon expression in planta. These mutant forms of I-2 were found to be impaired in ATP hydrolysis, but not in ATP binding, suggesting that the ATP- rather than the ADP-bound state of I-2 is the active form that triggers defense signaling. In addition, upon ADP binding, the protein displayed an increased affinity for ADP suggestive of a change of conformation. Based on these data, we propose that the NB-ARC domain of I-2, and likely of related R proteins, functions as a molecular switch whose state (on/off) depends on the nucleotide bound (ATP/ADP). 相似文献
6.
Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana.
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Calreticulin (CRT) is a calcium-binding protein in the endoplasmic reticulum (ER) with an established role as a molecular chaper-one. An additional function in signal transduction, specifically in calcium distribution, is suggested but not proven. We have analyzed the expression pattern of Arabidopsis thaliana CRTs for a comparison with these proposed roles. Three CRT genes were expressed, with identities of the encoded proteins ranging from 54 to 86%. Protein motifs with established functions found in CRTs of other species were conserved. CRT was found in all of the cells in low amounts, whereas three distinct floral tissues showed abundant expression: secreting nectaries, ovules early in development, and a set of subepidermal cells near the abaxial surface of the anther. Localization in the developing endosperm, which is characterized by high protein synthesis rates, can be reconciled with a specific chaperone function. Equally, nectar production and secretion, a developmental stage marked by abundant ER, may require abundant CRT to accommodate the traffic of secretory proteins through the ER. Localization of CRT in the anthers, which are degenerating at the time of maximum expression of CRT, cannot easily be reconciled with a chaperone function but may indicate a role for CRT in anther maturation or dehiscence. 相似文献
7.
8.
Plants utilize tightly regulated mechanisms to defend themselves against pathogens. Initial recognition results in activation of specific Resistance (R) proteins that trigger downstream immune responses, in which the signaling networks remain largely unknown. A point mutation in SUPPRESSOR OF NPR1 CONSTITUTIVE1 (SNC1), a RESISTANCE TO PERONOSPORA PARASITICA4 R gene homolog, renders plants constitutively resistant to virulent pathogens. Genetic suppressors of snc1 may carry mutations in genes encoding novel signaling components downstream of activated R proteins. One such suppressor was identified as a novel loss-of-function allele of ENHANCED RESPONSE TO ABSCISIC ACID1 (ERA1), which encodes the beta-subunit of protein farnesyltransferase. Protein farnesylation involves attachment of C15-prenyl residues to the carboxyl termini of specific target proteins. Mutant era1 plants display enhanced susceptibility to virulent bacterial and oomycete pathogens, implying a role for farnesylation in basal defense. In addition to its role in snc1-mediated resistance, era1 affects several other R-protein-mediated resistance responses against bacteria and oomycetes. ERA1 acts partly independent of abscisic acid and additively with the resistance regulator NON-EXPRESSOR OF PR GENES1 in the signaling network. Defects in geranylgeranyl transferase I, a protein modification similar to farnesylation, do not affect resistance responses, indicating that farnesylation is most likely specifically required in plant defense signaling. Taken together, we present a novel role for farnesyltransferase in plant-pathogen interactions, suggesting the importance of protein farnesylation, which contributes to the specificity and efficacy of signal transduction events. 相似文献
9.
Thomas W. H. Liebrand Anja Kombrink Zhao Zhang Jan Sklenar Alexandra M. E. Jones Silke Robatzek Bart P. H. J. Thomma Matthieu H. A. J. Joosten 《Molecular Plant Pathology》2014,15(1):109-117
The tomato receptor‐like protein (RLP) Ve1 mediates resistance to the vascular fungal pathogen Verticillium dahliae. To identify the proteins required for Ve1 function, we transiently expressed and immunopurified functional Ve1‐enhanced green fluorescent protein (eGFP) from Nicotiana benthamiana leaves, followed by mass spectrometry. This resulted in the identification of peptides originating from the endoplasmic reticulum (ER)‐resident chaperones HSP70 binding proteins (BiPs) and a lectin‐type calreticulin (CRT). Knock‐down of the different BiPs and CRTs in tomato resulted in compromised Ve1‐mediated resistance to V. dahliae in most cases, showing that these chaperones play an important role in Ve1 functionality. Recently, it has been shown that one particular CRT is required for the biogenesis of the RLP‐type Cladosporium fulvum resistance protein Cf‐4 of tomato, as silencing of CRT3a resulted in a reduced pool of complex glycosylated Cf‐4 protein. In contrast, knock‐down of the various CRTs in N. benthamiana or N. tabacum did not result in reduced accumulation of mature complex glycosylated Ve1 protein. Together, this study shows that the BiP and CRT ER chaperones differentially contribute to Cf‐4‐ and Ve1‐mediated immunity. 相似文献
10.
Liebrand TW Smit P Abd-El-Haliem A de Jonge R Cordewener JH America AH Sklenar J Jones AM Robatzek S Thomma BP Tameling WI Joosten MH 《Plant physiology》2012,159(4):1819-1833
Cf proteins are receptor-like proteins (RLPs) that mediate resistance of tomato (Solanum lycopersicum) to the foliar pathogen Cladosporium fulvum. These transmembrane immune receptors, which carry extracellular leucine-rich repeats that are subjected to posttranslational glycosylation, perceive effectors of the pathogen and trigger a defense response that results in plant resistance. To identify proteins required for the functionality of these RLPs, we performed immunopurification of a functional Cf-4-enhanced green fluorescent protein fusion protein transiently expressed in Nicotiana benthamiana, followed by mass spectrometry. The endoplasmic reticulum (ER) heat shock protein70 binding proteins (BiPs) and lectin-type calreticulins (CRTs), which are chaperones involved in ER-quality control, were copurifying with Cf-4-enhanced green fluorescent protein. The tomato and N. benthamiana genomes encode four BiP homologs and silencing experiments revealed that these BiPs are important for overall plant viability. For the three tomato CRTs, virus-induced gene silencing targeting the plant-specific CRT3a gene resulted in a significantly compromised Cf-4-mediated defense response and loss of full resistance to C. fulvum. We show that upon knockdown of CRT3a the Cf-4 protein accumulated, but the pool of Cf-4 protein carrying complex-type N-linked glycans was largely reduced. Together, our study on proteins required for Cf function reveals an important role for the CRT ER chaperone CRT3a in the biogenesis and functionality of this type of RLP involved in plant defense. 相似文献
11.
Sally D. Warring Zhicheng Dou Vern B. Carruthers Geoffrey I. McFadden Giel G. van Dooren 《Eukaryotic cell》2014,13(11):1360-1370
Mutations in the Plasmodium falciparum chloroquine resistance transporter (PfCRT) protein confer resistance to the antimalarial drug chloroquine. PfCRT localizes to the parasite digestive vacuole, the site of chloroquine action, where it mediates resistance by transporting chloroquine out of the digestive vacuole. PfCRT belongs to a family of transporter proteins called the chloroquine resistance transporter family. CRT family proteins are found throughout the Apicomplexa, in some protists, and in plants. Despite the importance of PfCRT in drug resistance, little is known about the evolution or native function of CRT proteins. The apicomplexan parasite Toxoplasma gondii contains one CRT family protein. We demonstrate that T. gondii CRT (TgCRT) colocalizes with markers for the vacuolar (VAC) compartment in these parasites. The TgCRT-containing VAC is a highly dynamic organelle, changing its morphology and protein composition between intracellular and extracellular forms of the parasite. Regulated knockdown of TgCRT expression resulted in modest reduction in parasite fitness and swelling of the VAC, indicating that TgCRT contributes to parasite growth and VAC physiology. Together, our findings provide new information on the role of CRT family proteins in apicomplexan parasites. 相似文献
12.
Kobayashi S Uchiyama S Sone T Noda M Lin L Mizuno H Matsunaga S Fukui K 《Cytogenetic and genome research》2006,115(1):10-15
Calreticulin (CRT) is a multifunctional Ca(2+)-binding protein that mainly functions in the endoplasmic reticulum as a molecular chaperone for newly synthesized proteins. Recently we reported the protein composition of human metaphase chromosomes (Uchiyama et al., 2004), which included CRT. Here we describe new characteristics of CRT in vitro as well as its localization on the surface of metaphase chromosomes in vivo. CRT was detected in the chromosomal fraction by Western blotting and its binding partners were identified as core and linker histones by ligand overlay assay. Surface plasmon resonance sensor analyses revealed that CRT is bound to chromatin fibers. Moreover, we found that CRT has both supercoiling activity, which assists core histone assembly into chromatin fibers, and binding ability to histone H2A/H2B dimers and histone H3/H4 tetramers. Unlike the chromosome scaffold proteins, indirect immunofluorescent staining revealed that CRT is located on the surface of metaphase chromosomes. These results suggest that CRT plays a role which involves chromatin dynamics on the surface of mitotic chromosomes. 相似文献
13.
Katarzyna Popłońska 《Protoplasma》2013,250(1):43-51
During spermiogenesis of an alga Chara vulgaris, which resembles that of animals, nucleohistones are replaced by protamine-type proteins. This exchange takes place in a spermatid nucleus during the key V spermiogenesis stage, in which rough endoplasmic reticulum is the site of protamine-type protein synthesis and is also the pathway guiding the proteins to their destination, nucleus. In the present work, it was shown that a chaperon protein, calreticulin (CRT), abundantly present at this significant V stage of spermiogenesis in a few cellular compartments, i.e., a nucleus, lumen of cisternae, and vesicles of significantly swollen ER as well as outside these structures, e.g., in Golgi apparatus, could have taken part in the process of exchange of nuclear proteins. Colocalization of two proteins, protamine-type proteins, crucial for reproduction, and CRT, was especially visible in a nucleus, mainly on its peripheries where condensed chromatin was present. Localization of protamine-type proteins and CRT in nucleus is in agreement with our previous results showing that protamine-type proteins were twofold more labelled in the peripheral area in comparison to the nucleus center occupied by noncondensed chromatin. The role of CRT in the reproduction of both plants and animals is also discussed. 相似文献
14.
p38丝裂素活化蛋白激酶介导低氧预处理诱导的内质网应激相关的心肌细胞保护 总被引:12,自引:2,他引:10
钙网蛋白(calreticulin,CRT)和caspase-12是重要的内质网(endoplasmic reticulum,ER)应激分子,本实验在心肌细胞低氧/复氧(hypoxia/reoxygenation,H/R)模型上观察低氧预处理(hypoxic preconditioning,HPC)对CRT和caspase-12表达及活化的影响,探讨内质网应激(endoplasmic reticulum stress,ERS)在HPC保护机制中的意义及其细胞信号转导机制。原代培养的Sprague-Dawley乳鼠心肌细胞随机分为6组:H/R组、HPC+H/R组、SB203580+HPC+H/R组、SP600125+HPC+H/R组、HPC组和对照组。以细胞存活率、乳酸脱氢酶(lactate dehydrogenase,LDH)活性及流式细胞术检测细胞损伤情况:Western blot方法检测CRT和caspase-12表达、活化及p38丝裂素活化蛋白激酶(mitogen—activated protein kinases,MAPK)、cJun N-terminal kinase(JNK)磷酸化水平。结果表明:(1)HPC具有细胞保护作用,与H/R组比较,HPC+H/R组细胞凋亡率和LDH漏出分别降低6.6%和70.0%,存活率增高6.4%:HPC前以特异性p38MAPK抑制剂SB203580预孵育消除HPC的保护作用,与HPC+H/R组相比,细胞凋亡率和LDH漏出分别增高5.4%和2.1倍,存活率降低5.4%,JNK特异性抑制剂SP600125预孵育对HPC的保护作用无明显影响。(2)H/R明显上调CRT表达(较对照组高8.1倍)和caspase-12活性(较对照组高33.2倍);单独HPC可诱导CRT表达增多(较对照组高2.6倍),但上调程度较H/R组低60%。H/R前进行HPC降低CRT过表达程度(降低72.4%)及caspase-12活化水平(降低59.6%)。(3)HPC前应用p38MAPK抑制剂,抑制CRT表达上调(分别较HPC+H/R组和HPC组低63.9%和71.9%),并消除HPC减轻H/R上调caspase-12活性的作用(较HPC+H/R组高7.1倍);HPC前抑制JNK活性对CRT、caspase-12表达和活化均无明显影响。上述结果提示:HPC可激发适当的ERS,抑制H/R诱导的过度ERS,减少ER凋亡信号介导的细胞凋亡。p38MAPK信号途径在HPC诱导的ER应激分子表达、抑制ER凋亡信号分子活化等机制中发挥重要作用。 相似文献
15.
Calreticulin induces delayed cardioprotection through mitogen-activated protein kinases 总被引:7,自引:0,他引:7
Hypoxic preconditioning (HPC) attenuates tissue injury caused by ischemia/reperfusion. The protective mechanisms of HPC involve up-regulation of the protective proteins and mitigation of cellular calcium overload. Calreticulin (CRT), a Ca(2+)-binding chaperone, plays an important role in regulating calcium homeostasis and folding of proteins. The role of CRT in cardioprotection of HPC and the pathways determining CRT expression during HPC are not clear. In this work, 2-DE and MALDI-MS were employed to analyze CRT differential expression in cardiomyocytes subjected to transient hypoxia. Western blotting analysis was used to detect the CRT expression and activities of p38 mitogen-activated protein kinase (p38 MAPK) and c-Jun NH(2)-terminal kinase (JNK) in myocardium subjected to ischemia with and without HPC and sham operation. The hearts from HPC group were more resistant to sustained ischemia and had much stronger phosphorylation of p38 MAPK, with a reduced phosphorylation of JNK, than controls. The CRT expression was positively correlated with the phosphorylation of p38 MAPK and negatively correlated with the level of JNK phosphorylation. Furthermore, inhibition of the p38 MAPK with SB202190 abolished, while inhibition of the JNK with SP600125 enhanced the CRT up-regulation in cardiomyocytes induced by HPC. The results indicate that HPC up-regulates CRT expression through the MAPK signaling pathways. 相似文献
16.
Transportin-SR is required for proper splicing of resistance genes and plant immunity 总被引:1,自引:0,他引:1
Transportin-SR (TRN-SR) is a member of the importin-β super-family that functions as the nuclear import receptor for serine-arginine rich (SR) proteins, which play diverse roles in RNA metabolism. Here we report the identification and cloning of mos14 (modifier of snc1-1, 14), a mutation that suppresses the immune responses conditioned by the auto-activated Resistance (R) protein snc1 (suppressor of npr1-1, constitutive 1). MOS14 encodes a nuclear protein with high similarity to previously characterized TRN-SR proteins in animals. Yeast two-hybrid assays showed that MOS14 interacts with AtRAN1 via its N-terminus and SR proteins via its C-terminus. In mos14-1, localization of several SR proteins to the nucleus was impaired, confirming that MOS14 functions as a TRN-SR. The mos14-1 mutation results in altered splicing patterns of SNC1 and another R gene RPS4 and compromised resistance mediated by snc1 and RPS4, suggesting that nuclear import of SR proteins by MOS14 is required for proper splicing of these two R genes and is important for their functions in plant immunity. 相似文献
17.
Plant disease resistance is the consequence of an innate defense mechanism mediated by Resistance (R) genes [1]. The conserved structure of one class of R protein is reminiscent of Toll-like receptors (TLRs) and Nucleotide binding oligomerization domain (NOD) proteins-immune-response perception modules in animal cells [2, 3, and 4]. The Arabidopsis snc1 (suppressor of npr1-1, constitutive, 1) mutant contains a mutation in a TIR-NBS-LRR-type of R gene that renders resistance responses constitutively active without interaction with pathogens [5]. Few components of the downstream signaling network activated by snc1 are known. To search for regulators of R-gene-mediated resistance, we screened for genetic suppressors of snc1. Three alleles of the mutant mos6 (modifier of snc1, 6) partially suppressed constitutive-resistance responses and immunity to virulent pathogens in snc1. Furthermore, the mos6-1 single mutant exhibited enhanced disease susceptibility to a virulent oomycete pathogen. MOS6, identified by positional cloning, encodes importin alpha3, one of eight alpha importins in Arabidopsis [6]. alpha importins mediate the import of specific proteins across the nuclear envelope. We previously reported that MOS3, a protein homologous to human nucleoporin 96, is required for constitutive resistance in snc1 [7]. Our data highlight an essential role for nucleo-cytoplasmic trafficking, especially protein import, in plant innate immunity. 相似文献
18.
Calreticulin, a potential cell surface receptor involved in cell penetration of anti-DNA antibodies 总被引:2,自引:0,他引:2
Seddiki N Nato F Lafaye P Amoura Z Piette JC Mazié JC 《Journal of immunology (Baltimore, Md. : 1950)》2001,166(10):6423-6429
A 50-kDa protein was purified as a potential receptor, using an affinity matrix containing biotinylated F14.6 or H9.3 anti-DNA mAbs derived from autoimmune (New Zealand Black x New Zealand White)F(1) mouse and membrane extracts from cells. This protein was identified as calreticulin (CRT) by microsequencing. Confocal microscopy and FACS analysis showed that CRT was present on the surface of various cells. CRT protein was recognized by a panel of anti-DNA mAbs in ELISA. The binding of F14.6 to lymphocytes and Chinese hamster ovary cells was inhibited by soluble CRT or SPA-600. Thus, the anti-DNA mAbs used in this study bound to CRT, suggesting that CRT may mediate their penetration into the cells and play an important role in lupus pathogenesis. 相似文献
19.
植物抗病基因结构、功能及其进化机制研究进展 总被引:9,自引:0,他引:9
植物与病原菌在长期的共进化和相互选择的过程中,逐渐形成了组织障碍、非寄主抗性和小种专化抗性等有效的防御机制。小种专化抗性(基因对基因抗性)主要是由植物抗病基因识别相应的病原菌无毒基因并激活植物体内抗病信号进而抵御病原菌的侵染。从目前已克隆的 70 多个抗病基因来看,它们在结构上具有高度保守性,主要包括核苷酸结合位点(NBS),亮氨酸重复结构(LRR), 蛋白激酶结构域(PK), 果蝇蛋白 Toll 和哺乳动物蛋白质白细胞介素 1 受体[interleukin(IL)-1 receptor]类似结构域(TIR), 双螺旋结构(CC)或亮氨酸拉链(LZ)和跨膜结构域(TM)等,其在抗病基因与病原菌无毒(效应)蛋白互作以及植物内部免疫信号传导中起着重要的作用。同时,抗病基因又通过基因复制、遗传重组等进化机制形成多基因家族,为植物抗病的专化性和多样性提供了重要的遗传基础。本文主要讨论了近来已克隆抗病基因的结构特征、功能以及抗病基因进化机制研究的进展。 相似文献