scholarly journals CDC42 (cell division cycle 42 (GTP binding protein, 25kDa))

2011 ◽  
Author(s):  
F Valdés-Mora ◽  
del Pulgar T Gómez ◽  
JC Lacal
Keyword(s):  
Cell Division ◽  
Binding Protein ◽  
Cell Division Cycle ◽  
Gtp Binding Protein ◽  
Gtp Binding

A Role for the Common GTP-Binding Protein in Coupling of Chromosome Replication to Cell Growth and Cell Division

2002 ◽  
Vol 292 (2) ◽  
pp. 333-338 ◽  
Author(s):  
Aleksandra Sikora-Borgula ◽  
Monika Słomińska ◽  
Piotr Trzonkowski ◽  
Ryszard Zielke ◽  
Andrzej Myśliwski ◽  
...  
Keyword(s):  
Cell Division ◽  
Cell Growth ◽  
Binding Protein ◽  
Chromosome Replication ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
The Common

Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein

Nature ◽  
1992 ◽  
Vol 359 (6392) ◽  
pp. 251-254 ◽  
Author(s):  
Debabrata RayChaudhuri ◽  
James T. Park
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Binding Protein ◽  
Coli Cell ◽  
Gtp Binding Protein ◽  
Gtp Binding

Impaired chromosome partitioning and synchronization of DNA replication initiation in an insertional mutant in the Vibrio harveyi cgtA gene coding for a common GTP-binding protein

2002 ◽  
Vol 362 (3) ◽  
pp. 579-584 ◽  
Author(s):  
Monika SŁOMIṄSKA ◽  
Grażyna KONOPA ◽  
Grzegorz WĘGRZYN ◽  
Agata CZYŻ
Keyword(s):  
Cell Division ◽  
Gene Product ◽  
Vibrio Harveyi ◽  
Binding Protein ◽  
Chromosome Replication ◽  
Replication Initiation ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Insertional Mutant ◽  
Chromosome Partitioning

The Vibrio harveyi cgtA gene product belongs to a subfamily of small GTP-binding proteins, called Obg-like proteins. Members of this subfamily are present in diverse organisms ranging from bacteria to humans. On the other hand, the functions of these proteins in the regulation of cellular processes are largely unknown. Genes coding for these proteins are essential in almost all bacteria investigated thus far. However, a viable V. harveyi insertional mutant in the cgtA gene was described recently. Therefore, this mutant gives a unique opportunity to study functions of a member of the subfamily of Obg-like proteins. Here we demonstrate that the mutant cells often form long filaments with expanded, non-partitioned or rarely partitioned chromosomes. Such a phenotype suggests impairment of the mechanism of chromosome partition. Flow cytometric studies revealed that synchronization of chromosome replication initiation is also significantly disturbed in the cgtA mutant. Moreover, in contrast to wild-type V. harveyi, inhibition of chromosome replication and/or of cell division in the mutant bacteria caused significant increase in the number of large cells, suggesting that the cgtA gene product may be involved in the coupling of cell growth to chromosome replication and cell division. These results indicate that CgtA, an Obg-like GTP-binding protein, plays an important role in the regulation of chromosomal functions.

Recruitment of the Earliest Component of the Bacterial Flagellum to the Old Cell Division Pole by a Membrane-Associated Signal Recognition Particle Family GTP-Binding Protein

2009 ◽  
Vol 391 (4) ◽  
pp. 679-690 ◽  
Author(s):  
Johnathan C.D. Green ◽  
Christina Kahramanoglou ◽  
Alamgir Rahman ◽  
Alexandra M.C. Pender ◽  
Nicolas Charbonnel ◽  
...  
Keyword(s):  
Cell Division ◽  
Binding Protein ◽  
Signal Recognition Particle ◽  
Signal Recognition ◽  
Gtp Binding Protein ◽  
Bacterial Flagellum ◽  
Gtp Binding

Small GTP-binding Protein RalA Associates with Weibel-Palade Bodies in Endothelial Cells

1999 ◽  
Vol 82 (09) ◽  
pp. 1177-1181 ◽  
Author(s):  
Hubert de Leeuw ◽  
Pauline Wijers-Koster ◽  
Jan van Mourik ◽  
Jan Voorberg
Keyword(s):  
Endothelial Cells ◽  
Binding Proteins ◽  
Binding Protein ◽  
Control Release ◽  
Small Gtpase ◽  
Gtp Binding Protein ◽  
Two Dimensional Gel Electrophoresis ◽  
Gtp Binding Proteins ◽  
Dense Granules ◽  
Gtp Binding

SummaryIn endothelial cells von Willebrand factor (vWF) and P-selectin are stored in dense granules, so-called Weibel-Palade bodies. Upon stimulation of endothelial cells with a variety of agents including thrombin, these organelles fuse with the plasma membrane and release their content. Small GTP-binding proteins have been shown to control release from intracellular storage pools in a number of cells. In this study we have investigated whether small GTP-binding proteins are associated with Weibel-Palade bodies. We isolated Weibel-Palade bodies by centrifugation on two consecutive density gradients of Percoll. The dense fraction in which these subcellular organelles were highly enriched, was analysed by SDS-PAGE followed by GTP overlay. A distinct band with an apparent molecular weight of 28,000 was observed. Two-dimensional gel electrophoresis followed by GTP overlay revealed the presence of a single small GTP-binding protein with an isoelectric point of 7.1. A monoclonal antibody directed against RalA showed reactivity with the small GTP-binding protein present in subcellular fractions that contain Weibel-Palade bodies. The small GTPase RalA was previously identified on dense granules of platelets and on synaptic vesicles in nerve terminals. Our observations suggest that RalA serves a role in regulated exocytosis of Weibel-Palade bodies in endothelial cells.

Rap1b Association with the Platelet Cytoskeleton Occurs in the Absence of Glycoproteins IIb/IIIa

1998 ◽  
Vol 79 (04) ◽  
pp. 832-836 ◽  
Author(s):  
Thomas Fischer ◽  
Christina Duffy ◽  
Gilbert White
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Binding Proteins ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Gtp Binding Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

SummaryPlatelet membrane glycoproteins (GP) IIb/IIIa and rap1b, a 21 kDa GTP binding protein, associate with the triton-insoluble, activation-dependent platelet cytoskeleton with similar rates and divalent cation requirement. To examine the possibility that GPIIb/IIIa was required for rap1b association with the cytoskeleton, experiments were performed to determine if the two proteins were linked under various conditions. Chromatography of lysates from resting platelets on Sephacryl S-300 showed that GPIIb/IIIa and rap1b were well separated and distinct proteins. Immunoprecipitation of GPIIb/IIIa from lysates of resting platelets did not produce rap1b or other low molecular weight GTP binding proteins and immunoprecipitation of rap1b from lysates of resting platelets did not produce GPIIb/IIIa. Finally, rap1b was associated with the activation-dependent cytoskeleton of platelets from a patient with Glanzmann’s thrombasthenia who lacks surface expressed glycoproteins IIb and IIIa. Based on these findings, we conclude that no association between GPIIb/IIIa and rap1b is found in resting platelets and that rap1b association with the activation-dependent cytoskeleton is at least partly independent of GPIIb/IIIa.

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