4.5 Article

Association of human DNA helicase RecQ5β with RNA polymerase II and its possible role in transcription

Journal

BIOCHEMICAL JOURNAL
Volume 413, Issue -, Pages 505-516

Publisher

PORTLAND PRESS LTD
DOI: 10.1042/BJ20071392

Keywords

functional proteomics; gene regulation; protein-protein interaction; RecQ5 beta; RNA polymerase II (RNAP II); transcription

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Although RecQ5 beta is a ssDNA (single-stranded DNA)-stimulated ATPase and an ATP-dependent DNA helicase with strand-annealing activities, its cellular function remains to be explored. In the present paper, we used immunopurification and MS-based analyses to show that human DNA helicase RecQ5 beta is associated with at least four RNAP II (RNA polymerase II) subunits. RecQ5 beta was also present in complexes immunoprecipitated using three different antibodies against the large subunit of RNAP II, or in complexes immunoprecipitated using an anti-FLAG antibody against either FLAG-RNAP II 33 kDa subunit or FLAG-Pin 1. Different regions of the non-helicase domain of the RecQ5 beta molecule were associated with hypophosphorylated and hyperphosphorylated forms of the RNAP II large subunit independently of DNA and RNA. RecQ5 beta was also found in nuclear chromatin fractions and associated with the coding regions of the LDL (low-density lipoprotem) receptor and beta-actin genes. Knockdown of the RecQ5 beta transcript increased the transcription of those genes. The results of the present study suggest that RecQ5 beta has suppressive roles in events associated with RNAP II-dependent transcription.

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