Cooperative binding of the hnRNP K three KH domains to mRNA targets

13 October 2004

journal article
Published by Wiley in FEBS Letters

Vol. 577 (1-2) , 134-140
https://doi.org/10.1016/j.febslet.2004.08.086

Abstract

The heterogeneous nuclear ribonucleoprotein (hnRNP) K homology (KH) domain is an evolutionarily conserved module that binds short ribonucleotide sequences. KH domains most often are present in multiple copies per protein. In vitro studies of hnRNP K and other KH domain bearing proteins have yielded conflicting results regarding the relative contribution of each KH domain to the binding of target RNAs. To assess this RNA-binding we used full-length hnRNP K, its fragments and the yeast ortholog as baits in the yeast three-hybrid system. The results demonstrate that in this heterologous in vivo system, the three KH domains bind RNA synergistically and that a single KH domain, in comparison, binds RNA weakly.

Keywords

This publication has 39 references indexed in Scilit:

RNA regulation: a new genetics?
Nature Reviews Genetics, 2004
Messenger-RNA-binding proteins and the messages they carry
Nature Reviews Molecular Cell Biology, 2002
The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
RNA, 2002
KH domain: one motif, two folds
Nucleic Acids Research, 2001
Initial sequencing and analysis of the human genome
Nature, 2001
Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains
European Journal of Biochemistry, 1996
Cloning and characterization of a single-stranded DNA binding protein that specifically recognizes deoxycytidine stretch
Nucleic Acids Research, 1994
The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
Cell, 1993
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, 1993
The pre-mRNA binding K protein contains a novel evolutionary conserved motif
Nucleic Acids Research, 1993