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PMID: 8405383 Published · ppublish English Comparative Study Journal Article

The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid.

FEBS letters ·Vol. 324 ·No. 3 ·1993-06-21 ·Pages 361-6

Gibson TJ, Thompson JD, Heringa J

Abstract

New findings are presented for the approximately 50 residue KH motif, a domain recently discovered in RNA-binding proteins. The conserved sequence is approximately 10 residues larger than previously reported. Profile searches have revealed new members of this family, including two, E. coli NusA and human GAP-associated p62 phosphoprotein, for which RNA-binding data exists. A nusA homolog was detected in the RNA polymerase gene complex of six archaebacterial species and may encode an antiterminator. All KH-containing proteins are linked with RNA and the KH motif most probably functions as a nucleic acid binding domain.

Related Genes
MeSH Terms
Bacterial Proteins/chemistry Escherichia coli Proteins Molecular Sequence Data Peptide Elongation Factors RNA-Binding Proteins/chemistry Repetitive Sequences, Nucleic Acid Sequence Alignment Sequence Homology, Amino Acid Transcription Factors/chemistry Transcriptional Elongation Factors
Chemicals
Bacterial Proteins Escherichia coli Proteins Peptide Elongation Factors RNA-Binding Proteins Transcription Factors Transcriptional Elongation Factors nusA protein, E coli
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gibson T J
European Molecular Biology Laboratory, Heidelberg, Germany.
Thompson J D
Heringa J
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1993-06-21
Pages
361-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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