Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the holliday junction

1998 ◽  
Vol 278 (1) ◽  
pp. 105-116 ◽  
Author(s):  
John B Rafferty ◽  
Stuart M Ingleston ◽  
David Hargreaves ◽  
Peter J Artymiuk ◽  
Gary J Sharples ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Proteins ◽  
Mutational Analysis ◽  
Dna Binding Proteins ◽  
Holliday Junction

scholarly journals Analysis of the Role oftrans-Translation in the Requirement of tmRNA for λimmP22 Growth in Escherichia coli

1999 ◽  
Vol 181 (7) ◽  
pp. 2148-2157 ◽  
Author(s):  
Jeffrey Withey ◽  
David Friedman
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Proteins ◽  
Mutational Analysis ◽  
Dna Binding Proteins ◽  
Peptide Sequence ◽  
Primary Role ◽  
Translation Model ◽  
Small Stable Rna

ABSTRACT The small, stable RNA molecule encoded by ssrA, known as tmRNA or 10Sa RNA, is required for the growth of certain hybrid λimm P22 phages in Escherichia coli. tmRNA has been shown to tag partially synthesized proteins for degradation in vivo by attaching a short peptide sequence, encoded by tmRNA, to the carboxyl termini of these proteins. This tag sequence contains, at its C terminus, an amino acid sequence that is recognized by cellular proteases and leads to degradation of tagged proteins. A model describing this function of tmRNA, thetrans-translation model (K. C. Keiler, P. R. Waller, and R. T. Sauer, Science 271:990–993, 1996), proposes that tmRNA acts first as a tRNA and then as a mRNA, resulting in release of the original mRNA template from the ribosome and translocation of the nascent peptide to tmRNA. Previous work from this laboratory suggested that tmRNA may also interact specifically with DNA-binding proteins, modulating their activity. However, more recent results indicate that interactions between tmRNA and DNA-binding proteins are likely nonspecific. In light of this new information, we examine the effects on λimm P22 growth of mutations eliminating activities postulated to be important for two different steps in the trans-translation model, alanine charging of tmRNA and degradation of tagged proteins. This mutational analysis suggests that, while charging of tmRNA with alanine is essential for λimm P22 growth in E. coli, degradation of proteins tagged by tmRNA is required only to achieve optimal levels of phage growth. Based on these results, we propose that trans-translation may have two roles, the primary role being the release of stalled ribosomes from their mRNA template and the secondary role being the tagging of truncated proteins for degradation.

scholarly journals Roles of the DNA binding proteins H-NS and StpA in homologous recombination and repair of bleomycin-induced damage in Escherichia coli

2007 ◽  
Vol 82 (5) ◽  
pp. 433-439 ◽  
Author(s):  
Kouya Shiraishi ◽  
Yasuyuki Ogata ◽  
Katsuhiro Hanada ◽  
Yasunobu Kano ◽  
Hideo Ikeda
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Homologous Recombination ◽  
Binding Proteins ◽  
Dna Binding Proteins

Studies with DNA-cellulose Chromatography. I. DNA-binding Proteins from Escherichia coli

1968 ◽  
Vol 33 (0) ◽  
pp. 289-305 ◽  
Author(s):  
B. M. Alberts ◽  
F. J. Amodio ◽  
M. Jenkins ◽  
E. D. Gutmann ◽  
F. L. Ferris
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins

scholarly journals Complete Amino-Acid Sequences of DNA-Binding Proteins HU-1 and HU-2 from Escherichia coli

1980 ◽  
Vol 103 (3) ◽  
pp. 456-461
Author(s):  
B. Laine ◽  
D. Kmiecik ◽  
P. Sautiere ◽  
G. Biserte ◽  
M. Cohen-Solal
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Amino Acid Sequences

Complete Amino-Acid Sequences of DNA-Binding Proteins HU-1 and HU-2 from Escherichia coli

1980 ◽  
Vol 103 (3) ◽  
pp. 447-461 ◽  
Author(s):  
Bernard LAINE ◽  
Daniel KMIECIK ◽  
Pierre SAUTIERE ◽  
Gerard BISERTE ◽  
Michel COHEN-SOLAL
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Amino Acid Sequences
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