Abstract
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.
Copyright 2004 Wiley-Liss, Inc.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Bacterial Proteins / chemistry*
-
Chromosomal Proteins, Non-Histone
-
Escherichia coli Proteins / chemistry
-
Haloarcula marismortui / chemistry
-
Models, Molecular
-
Molecular Sequence Data
-
Nuclear Magnetic Resonance, Biomolecular*
-
Peptide Elongation Factors / chemistry*
-
Protein Binding
-
Protein Structure, Secondary
-
Protein Structure, Tertiary
-
Ribosomal Proteins / chemistry
-
Sequence Alignment
-
Sequence Homology
-
Solutions
-
Surface Plasmon Resonance
-
Thermodynamics
-
Thermus thermophilus / chemistry*
-
Transcription Factors / chemistry*
-
Transcriptional Elongation Factors
Substances
-
Bacterial Proteins
-
Chromosomal Proteins, Non-Histone
-
Escherichia coli Proteins
-
NusG protein, E coli
-
Peptide Elongation Factors
-
Ribosomal Proteins
-
Solutions
-
Transcription Factors
-
Transcriptional Elongation Factors
-
ribosomal protein L24
-
SPT5 transcriptional elongation factor
-
nusG protein, Thermus thermophilus