scholarly journals The β-Subunit of the Signal Recognition Particle Receptor Is a Novel GTP-binding Protein without Intrinsic GTPase Activity

2003 ◽  
Vol 278 (30) ◽  
pp. 27712-27720 ◽  
Author(s):  
Kyle R. Legate ◽  
David W. Andrews
Keyword(s):  
Binding Protein ◽  
Signal Recognition Particle ◽  
Signal Recognition ◽  
Gtpase Activity ◽  
Β Subunit ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Signal Recognition Particle Receptor ◽  
Intrinsic Gtpase Activity

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

scholarly journals Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.

1986 ◽  
Vol 103 (6) ◽  
pp. 2253-2261 ◽  
Author(s):  
T Connolly ◽  
R Gilmore
Keyword(s):  
Signal Sequence ◽  
Binding Protein ◽  
Signal Recognition Particle ◽  
Secretory Protein ◽  
Signal Recognition ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Protease Digestion ◽  
Nascent Chain

The requirement for ribonucleotides and ribonucleotide hydrolysis was examined at several distinct points during translocation of a secretory protein across the endoplasmic reticulum. We monitored binding of in vitro-assembled polysomes to microsomal membranes after removal of ATP and GTP. Ribonucleotides were not required for the initial low salt-insensitive attachment of the ribosome to the membrane. However, without ribonucleotides the nascent secretory chains were sensitive to protease digestion and were readily extracted from the membrane with either EDTA or 0.5 M KOAc. In contrast, nascent chains resisted extraction with either EDTA or 0.5 M KOAc and were insensitive to protease digestion after addition of GTP or nonhydrolyzable GTP analogues. Translocation of the nascent secretory polypeptide was detected only when ribosome binding was conducted in the presence of GTP. Thus, translocation-competent binding of the ribosome to the membrane requires the participation of a novel GTP-binding protein in addition to the signal recognition particle and the signal recognition particle receptor. The second event we examined was translocation and processing of a truncated secretory polypeptide. Membrane-bound polysomes bearing an 86-residue nascent chain were generated by translation of a truncated preprolactin mRNA. Ribonucleotide-independent translocation of the polypeptide was detected by cleavage of the 30-residue signal sequence after puromycin termination. Nascent chain transport, per se, is apparently dependent upon neither ribonucleotide hydrolysis nor continued elongation of the polypeptide once a functional ribosome-membrane junction has been established.

scholarly journals Rac1, a low-molecular-mass GTP-binding-protein with high intrinsic GTPase activity and distinct biochemical properties

1992 ◽  
Vol 206 (2) ◽  
pp. 537-546 ◽  
Author(s):  
Luc MÉNARD ◽  
Eric TOMHAVE ◽  
Patric J. CASEY ◽  
Ronald J. UHING ◽  
Ralph SNYDERMAN ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Binding Protein ◽  
Biochemical Properties ◽  
Gtpase Activity ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Intrinsic Gtpase Activity

scholarly journals Rhodopsin-enhanced GTPase activity of the inhibitory GTP-binding protein of adenylate cyclase.

1984 ◽  
Vol 259 (12) ◽  
pp. 7378-7381 ◽  
Author(s):  
Y Kanaho ◽  
S C Tsai ◽  
R Adamik ◽  
E L Hewlett ◽  
J Moss ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Binding Protein ◽  
Gtpase Activity ◽  
Gtp Binding Protein ◽  
Gtp Binding

scholarly journals Characterization of GTPase Activity of TrmE, a Member of a Novel GTPase Superfamily, from Thermotoga maritima

2000 ◽  
Vol 182 (24) ◽  
pp. 7078-7082 ◽  
Author(s):  
Kunitoshi Yamanaka ◽  
Jihwan Hwang ◽  
Masayori Inouye
Keyword(s):  
Thermotoga Maritima ◽  
Binding Protein ◽  
Protein A ◽  
Hydrolysis Rate ◽  
Gtpase Activity ◽  
Gtp Binding Protein ◽  
Gene Encoding ◽  
Gtp Hydrolysis ◽  
Gtp Binding

ABSTRACT A gene encoding a putative GTP-binding protein, a TrmE homologue that is highly conserved in both prokaryotes and eukaryotes, was cloned from Thermotoga maritima, a hyperthermophilic bacterium.T. maritima TrmE was overexpressed in Escherichia coli and purified. TrmE has a GTPase activity but no ATPase activity. The GTPase activity can be competed with GTP, GDP, and dGTP but not with GMP, ATP, CTP, or UTP. Km andk cat at 70°C were 833 μM and 9.3 min−1, respectively. Our results indicate that TrmE is a GTP-binding protein with a very high intrinsic GTP hydrolysis rate. We also propose that TrmE homologues constitute a novel subfamily of the GTPase superfamily.

scholarly journals The Membrane-binding Motif of the Chloroplast Signal Recognition Particle Receptor (cpFtsY) Regulates GTPase Activity

2009 ◽  
Vol 284 (22) ◽  
pp. 14891-14903 ◽  
Author(s):  
Naomi J. Marty ◽  
Dakshinamurthy Rajalingam ◽  
Alicia D. Kight ◽  
Nathaniel E. Lewis ◽  
Daniel Fologea ◽  
...  
Keyword(s):  
Signal Recognition Particle ◽  
Membrane Binding ◽  
Binding Motif ◽  
Signal Recognition ◽  
Gtpase Activity ◽  
Signal Recognition Particle Receptor
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