排序方式: 共有47条查询结果,搜索用时 31 毫秒
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CENP-I is essential for centromere function in vertebrate cells 总被引:14,自引:0,他引:14
Nishihashi A Haraguchi T Hiraoka Y Ikemura T Regnier V Dodson H Earnshaw WC Fukagawa T 《Developmental cell》2002,2(4):463-476
We identified a novel essential centromere protein, CENP-I, which shows sequence similarity with fission yeast Mis6 protein, and we showed that CENP-I is a constitutive component of the centromere that colocalizes with CENP-A, -C, and -H throughout the cell cycle in vertebrate cells. To determine the precise function of CENP-I, we examined its role in centromere function by generating a conditional loss-of-function mutant in the chicken DT40 cell line. In the absence of CENP-I, cells arrested at prometaphase with misaligned chromosomes for long periods of time. Eventually, cells exited mitosis without undergoing cytokinesis. Immunocytochemical analysis of CENP-I-deficient cells demonstrated that both CENP-I and CENP-H are necessary for localization of CENP-C but not CENP-A to the centromere. 相似文献
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Tempting fate: BMP signals for cardiac morphogenesis 总被引:4,自引:0,他引:4
Heart muscle cell specification (cardiac myogenesis) and creating the four-chambered heart (cardiac morphogenesis) are subject to regulation, in certain model organisms, by bone morphogenetic proteins and their receptors. Extrapolation to mammals from organisms that develop outside the mother (flies, fish, frogs, and avians) has been confounded by very early lethality-at gastrulation-of many null alleles needed to prove cause-effect relations in this pathway. Here, we describe the use of lineage- or compartment-restricted null alleles as well as hypomorphic alleles, which circumvent these limitations and pinpoint novel essential functions for the bone morphogenetic protein cascade in mammalian cardiac development. 相似文献
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CENP-A is required for accurate chromosome segregation and sustained kinetochore association of BubR1 总被引:8,自引:0,他引:8
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Régnier V Vagnarelli P Fukagawa T Zerjal T Burns E Trouche D Earnshaw W Brown W 《Molecular and cellular biology》2005,25(10):3967-3981
CENP-A is an evolutionarily conserved, centromere-specific variant of histone H3 that is thought to play a central role in directing kinetochore assembly and in centromere function. Here, we have analyzed the consequences of disrupting the CENP-A gene in the chicken DT40 cell line. In CENP-A-depleted cells, kinetochore protein assembly is impaired, as indicated by mislocalization of the inner kinetochore proteins CENP-I, CENP-H, and CENP-C as well as the outer components Nuf2/Hec1, Mad2, and CENP-E. However, BubR1 and the inner centromere protein INCENP are efficiently recruited to kinetochores. Following CENP-A depletion, chromosomes are deficient in proper congression on the mitotic spindle and there is a transient delay in prometaphase. CENP-A-depleted cells further proceed through anaphase and cytokinesis with unequal chromosome segregation, suggesting that some kinetochore function remains following substantial depletion of CENP-A. We furthermore demonstrate that CENP-A-depleted cells exhibit a specific defect in maintaining kinetochore localization of the checkpoint protein BubR1 under conditions of checkpoint activation. Our data thus point to a specific role for CENP-A in assembly of kinetochores competent in the maintenance of mitotic checkpoint signaling. 相似文献
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Vigano C Grimard V Margolles A Goormaghtigh E van Veen HW Konings WN Ruysschaert JM 《FEBS letters》2002,530(1-3):197-203
LmrA confers multidrug resistance to Lactococcus lactis by mediating the extrusion of antibiotics, out of the bacterial membrane, using the energy derived from ATP hydrolysis. Cooperation between the cytosolic and membrane-embedded domains plays a crucial role in regulating the transport ATPase cycle of this protein. In order to demonstrate the existence of a structural coupling required for the cross-talk between drug transport and ATP hydrolysis, we studied specifically the dynamic changes occurring in the membrane-embedded and cytosolic domains of LmrA by combining infrared linear dichroic spectrum measurements in the course of H/D exchange with Trp fluorescence quenching by a water-soluble attenuator. This new experimental approach, which is of general interest in the study of membrane proteins, detects long-range conformational changes, transmitted between the membrane-embedded and cytosolic regions of LmrA. On the one hand, nucleotide binding and hydrolysis in the cytosolic nucleotide binding domain cause a repacking of the transmembrane helices. On the other hand, drug binding to the transmembrane helices affects both the structure of the cytosolic regions and the ATPase activity of the nucleotide binding domain. 相似文献
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Régnier V Billard JM Gupta S Potier B Woerner S Paly E Ledru A David S Luilier S Bizot JC Vacano G Kraus JP Patterson D Kruger WD Delabar JM London J 《PloS one》2012,7(1):e29056