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Purification of a novel RECQL5-SWI/SNF-RNAPII super complex

  • Guangjin Zhou
  • , Yifei Liu
  • , Shwu Yuan Wu
  • , Feng Tie
  • , Hua Lou
  • , Cheng Ming Chiang
  • , Guangbin Luo

Research output: Contribution to journalArticlepeer-review

Abstract

RecQ helicases are members of an evolutionarily conserved family of DNA helicases. They are homologous to the RecQ helicase of E. coli, the founding member of the family. These enzymes include gene products of diseasecausing genes in Bloom, Werner, and Rothmund-Thomson syndrome. To date, these proteins have been implicated in many aspects of DNA metabolism, including DNA replication, repair, and recombination. We reported here that RECQL5, a newer member of the human RecQ helicase family, physically interacts with SWI/SNF complex and RNAPII core complex within the context of a super complex. RECQL5 was detected in the RNAPII holoenzyme but not in purified RNAPII core complex. Together, these data link RECQL5 to the assembly of the RNAPII transcription machinery and suggest that this helicase may have a regulatory role in RNAPII transcription or an RNAPII-related process or processes.

Original languageEnglish (US)
Pages (from-to)101-111
Number of pages11
JournalInternational Journal of Biochemistry and Molecular Biology
Volume1
Issue number1
StatePublished - 2010

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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