共查询到20条相似文献,搜索用时 15 毫秒
1.
2.
3.
4.
5.
6.
7.
The regulatory region of the human plasminogen activator inhibitor type-1 (PAI-1) gene. 总被引:5,自引:1,他引:4
下载免费PDF全文
![点击此处可从《Nucleic acids research》网站下载免费的PDF全文](/ch/ext_images/free.gif)
A Riccio L R Lund R Sartorio A Lania P A Andreasen K Dan F Blasi 《Nucleic acids research》1988,16(7):2805-2824
8.
9.
10.
Saumonneau A Rottier K Conrad U Popineau Y Guéguen J Francin-Allami M 《Plant cell reports》2011,30(7):1289-1302
In wheat, the high-molecular weight (HMW) glutenin subunits are known to contribute to gluten viscoelasticity, and show some
similarities to elastomeric animal proteins as elastin. When combining the sequence of a glutenin with that of elastin is
a way to create new chimeric functional proteins, which could be expressed in plants. The sequence of a glutenin subunit was
modified by the insertion of several hydrophobic and elastic motifs derived from elastin (elastin-like peptide, ELP) into
the hydrophilic repetitive domain of the glutenin subunit to create a triblock protein, the objective being to improve the
mechanical (elastomeric) properties of this wheat storage protein. In this study, we investigated an expression model system
to analyze the expression and trafficking of the wild-type HMW glutenin subunit (GSW) and an HMW glutenin subunit mutated by the insertion of elastin motifs (GSM-ELP). For this purpose, a series of constructs was made to express wild-type subunits and subunits mutated by insertion of
elastin motifs in fusion with green fluorescent protein (GFP) in tobacco BY-2 cells. Our results showed for the first time
the expression of HMW glutenin fused with GFP in tobacco protoplasts. We also expressed and localized the chimeric protein
composed of plant glutenin and animal elastin-like peptides (ELP) in BY-2 protoplasts, and demonstrated its presence in protein
body-like structures in the endoplasmic reticulum. This work, therefore, provides a basis for heterologous production of the
glutenin-ELP triblock protein to characterize its mechanical properties. 相似文献
11.
12.
13.
14.
Dumas B Centis S Sarrazin N Esquerré-Tugayé MT 《Applied and environmental microbiology》1999,65(4):1769-1771
The 5' noncoding region of clpg2, an endopolygalacturonase gene of the bean pathogen Colletotrichum lindemuthianum, was fused to the coding sequence of a gene encoding a green fluorescent protein (GFP), and the construct was introduced into the fungal genome. Detection of GFP accumulation by fluorescence microscopy examination revealed that clpg2 was expressed at the early stages of germination of the conidia and during appressorium formation both in vitro and on the host plant. 相似文献
15.
H Voss U Wirkner R Jakobi N A Hewitt C Schwager J Zimmermann W Ansorge W Pyerin 《The Journal of biological chemistry》1991,266(21):13706-13711
16.
17.
Peroxisomal catalase in the methylotrophic yeast Candida boidinii: transport efficiency and metabolic significance
下载免费PDF全文
![点击此处可从《Journal of bacteriology》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Horiguchi H Yurimoto H Goh T Nakagawa T Kato N Sakai Y 《Journal of bacteriology》2001,183(21):6372-6383
In this study we cloned CTA1, the gene encoding peroxisomal catalase, from the methylotrophic yeast Candida boidinii and studied targeting of the gene product, Cta1p, into peroxisomes by using green fluorescent protein (GFP) fusion proteins. A strain from which CTA1 was deleted (cta1Delta strain) showed marked growth inhibition when it was grown on the peroxisome-inducing carbon sources methanol, oleate, and D-alanine, indicating that peroxisomal catalase plays an important nonspecific role in peroxisomal metabolism. Cta1p carries a peroxisomal targeting signal type 1 (PTS1) motif, -NKF, in its carboxyl terminus. Using GFP fusion proteins, we found that (i) Cta1p is transported to peroxisomes via its PTS1 motif, -NKF; (ii) peroxisomal localization is necessary for Cta1p to function physiologically; and (iii) Cta1p is bimodally distributed between the cytosol and peroxisomes in methanol-grown cells but is localized exclusively in peroxisomes in oleate- and D-alanine-grown cells. In contrast, the fusion protein GFP-AKL (GFP fused to another typical PTS1 sequence, -AKL), in the context of CbPmp20 and D-amino acid oxidase, was found to localize exclusively in peroxisomes. A yeast two-hybrid system analysis suggested that the low transport efficiency of the -NKF sequence is due to a level of interaction between the -NKF sequence and the PTS1 receptor that is lower than the level of interaction with the AKL sequence. Furthermore, GFP-Cta1pDeltankf coexpressed with Cta1p was successfully localized in peroxisomes, suggesting that the oligomer was formed prior to peroxisome import and that it is not necessary for all four subunits to possess a PTS motif. Since the main physiological function of catalase is degradation of H2O2, suboptimal efficiency of catalase import may confer an evolutionary advantage. We suggest that the PTS1 sequence, which is found in peroxisomal catalases, has evolved in such a way as to give a higher priority for peroxisomal transport to peroxisomal enzymes other than to catalases (e.g., oxidases), which require a higher level of peroxisomal transport efficiency. 相似文献
18.
19.
20.
Thébault S Basbous J Gay B Devaux C Mesnard JM 《European journal of cell biology》2000,79(11):834-838
The human I-mfa domain-containing protein (HIC) mRNA produces two protein isoforms, HIC p32 and p40, synthesized from alternative translational initiations. p32 translation is initiated from a standard AUG codon and p40 is an N-terminal extension of p32 generated from an upstream GUG codon. The two isoforms show different subcellular localization: p32 is distributed throughout the cytoplasm whereas p40 can be found both in the cytoplasm and the nucleolus. To investigate the possibility that p40 contains a nucleolus targeting sequence in its N-terminal region, COS cells were transfected with an eukaryotic expression vector coding for green fluorescent protein (GFP) fused to the p40 N terminus. The localization of this fusion protein in the nucleolus indicated that the N-terminal amino acids of p40 probably contain a nucleolar localization signal (NoLS). To find the structural motifs required for nucleolar localization of p40, deletion mutants were expressed in COS cells as fusion polypeptides with GFP. We defined a domain of 19 amino acids near the N terminus that contains an arginine-rich subdomain that conforms to other known NoLS. To demonstrate that this sequence is an authentic NoLS, the sequence was fused to GFP. This fusion protein was observed to migrate into the nucleolus. Taken together, our studies demonstrate that p40 contains a NoLS. 相似文献