Publication Date:
2010-04-24
Description:
Bacterial NusG is a highly conserved transcription factor that is required for most Rho activity in vivo. We show by nuclear magnetic resonance spectroscopy that Escherichia coli NusG carboxyl-terminal domain forms a complex alternatively with Rho or with transcription factor NusE, a protein identical to 30S ribosomal protein S10. Because NusG amino-terminal domain contacts RNA polymerase and the NusG carboxy-terminal domain interaction site of NusE is accessible in the ribosomal 30S subunit, NusG may act as a link between transcription and translation. Uncoupling of transcription and translation at the ends of bacterial operons enables transcription termination by Rho factor, and competition between ribosomal NusE and Rho for NusG helps to explain why Rho cannot terminate translated transcripts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burmann, Bjorn M -- Schweimer, Kristian -- Luo, Xiao -- Wahl, Markus C -- Stitt, Barbara L -- Gottesman, Max E -- Rosch, Paul -- GM037219/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Apr 23;328(5977):501-4. doi: 10.1126/science.1184953.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl Biopolymere und Forschungszentrum fur Bio-Makromolekule, Universitat Bayreuth, Universitatsstrasse 30, 95447 Bayreuth, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20413501" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Binding Sites
;
Binding, Competitive
;
DNA-Directed RNA Polymerases/metabolism
;
Escherichia coli/genetics/*metabolism
;
Escherichia coli Proteins/biosynthesis/chemistry/*genetics/metabolism
;
Hydrophobic and Hydrophilic Interactions
;
Models, Molecular
;
Molecular Sequence Data
;
Nuclear Magnetic Resonance, Biomolecular
;
Operon
;
Peptide Elongation Factors/chemistry/*metabolism
;
Protein Binding
;
*Protein Biosynthesis
;
Protein Conformation
;
Protein Interaction Domains and Motifs
;
Protein Structure, Tertiary
;
Ribosomal Proteins/chemistry/*metabolism
;
Ribosome Subunits, Small, Bacterial/metabolism
;
Transcription Factors/chemistry/*metabolism
;
*Transcription, Genetic
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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