The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1

Cathelijne P.A.M. Kloks, Christian A.E.M. Spronk, Edwin Lasonder, Astrid Hoffmann, Geerten W. Vuister, Stephan Grzesiek, Cornelis W. Hilbers*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

92 Citations (Scopus)

Abstract

The human Y-box protein 1 (YB-1) is a member of the Y-box protein family, a class of proteins involved in transcriptional and translational regulation of a wide range of genes. Here, we report the solution structure of the cold-shock domain (CSD) of YB-1, which is thought to be responsible for nucleic acid binding. It is the first structure solved of a eukaryotic member of the cold-shock protein family and consists of a closed five-stranded anti-parallel β-barrel capped by a long flexible loop. The structure of CSD is similar to the OB-fold and a comparison with bacterial cold-shock proteins shows that its structural properties are conserved from bacteria to man. Our data suggest the presence of a DNA-binding site consisting of a patch of positively charged and aromatic residues on the surface of the β-barrel. Further, it is shown that CSD, which has a preference for binding single-stranded pyrimidine-rich sequences, binds weakly and hardly specifically to DNA. Binding affinities reported for intact YB-1 indicate that domains other than the CSD play a role in DNA binding of YB-1.

Original languageEnglish
Pages (from-to)317-326
Number of pages10
JournalJournal of Molecular Biology
Volume316
Issue number2
DOIs
Publication statusPublished - 15 Feb 2002
Externally publishedYes

Fingerprint Dive into the research topics of 'The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1'. Together they form a unique fingerprint.

Cite this