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 Lett. 1993 Jun 21;324(3):361-6. doi: 10.1016/0014-5793(93)80152-k.

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.

Publication types

  • Comparative Study

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

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Peptide Elongation Factors
  • RNA-Binding Proteins
  • Transcription Factors
  • Transcriptional Elongation Factors
  • nusA protein, E coli

Associated data

  • GENBANK/S74678