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

Heringa, Jaap¹  Gibson, Toby J.¹  Thompson, Julie D.¹ 

[1] European Molecular Biology Laboratory, Postfach 102209, Meyerhofstrasse 1, W-6900 Heidelberg, Germany

关键词: hnRNP;    Vigilin;    Ribosomal protein;    RNA polymerase;    3'-5' Exonuclease;    Profile search;    ORF;    open reading frame;    indel;    site of insertion or deletion in aligned sequences;    hnRNA;    heterogeneous nuclear RNA;    hnRNP;    protein associated with hnRNA;    KH;    domain with hnRNP K similarity;    5-APAS-UTP;    5-((4-azido-phenacyl)thio)-uridine-5' triphosphate;   

DOI  :  10.1016/0014-5793(93)80152-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

New findings are presented for the ~ 50 residue KH motif, a domain recently discovered in RNA-binding proteins. The conserved sequence is ~ 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 nus A 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.

【 授权许可】

Unknown