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Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus
Author(s) -
Reay Paul,
Yamasaki Kazuhiko,
Terada Takaho,
Kuramitsu Seiki,
Shirouzu Mikako,
Yokoyama Shigeyuki
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20054
Subject(s) - thermus thermophilus , elongation factor , biology , rna polymerase , structural similarity , peptide sequence , sequence (biology) , biochemistry , ef tu , transcription (linguistics) , rna , archaea , nucleic acid , genetics , escherichia coli , computational biology , transfer rna , ribosome , gene , linguistics , philosophy
NusG is an essential bacterial protein modulator of transcriptional elongation and termination events, and interacts directly with RNA polymerase and Rho protein. Found also in Archaea, NusG shows stretches of sequence similarity to the eukaryotic transcription elongation factor Spt5. Herein, the three‐dimensional solution structure of the bacterial NusG from Thermus thermophilus , which shows 43% amino acid sequence similarity to the Escherichia coli NusG, is described, and a survey of NusG and Spt5 amino acid sequences is presented. Although there is a clear evolutionary and functional relationship between these proteins, it is evident from the structural, sequence, and biochemical data that their binding specificities to both nucleic acids and other proteins differ. Proteins 2004. © 2004 Wiley‐Liss, Inc.