Int J Biochem Mol Biol 2010;1(1):101-111
Original Article
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
Department of Genetics, Case Western Reserve University, Cleveland, OH 44106, USA; Case Comprehensive Cancer Centre, University
Hospitals of Cleveland, Cleveland, OH 44106, USA; School of Life Sciences, Sun Yat-sen University, Guangzhou, China; Simmons
Comprehensive Cancer Center, Department of Biochemistry, and Department of Pharmacology, University of Texas Southwestern Medical
Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA
Received April 9, 2010; accepted April, 2010; available online April, 2010; published August 1, 2010
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 disease-causing 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. (IJBMB1004002).
Keywords:
Full Text PDF
Address all correspondence to:
Guangbin Luo, PhD
Department of Genetics, School of Medicine
Case Western Reserve University
Biomedical Research Building 720
2109 Adelbert Road, Cleveland, OH 44106-4955, USA.
Tel: 1-(216)-368-4883; Fax: 1-(216)-368-3432
E-mail: guangbin.luo@case.edu
Original Article
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
Department of Genetics, Case Western Reserve University, Cleveland, OH 44106, USA; Case Comprehensive Cancer Centre, University
Hospitals of Cleveland, Cleveland, OH 44106, USA; School of Life Sciences, Sun Yat-sen University, Guangzhou, China; Simmons
Comprehensive Cancer Center, Department of Biochemistry, and Department of Pharmacology, University of Texas Southwestern Medical
Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA
Received April 9, 2010; accepted April, 2010; available online April, 2010; published August 1, 2010
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 disease-causing 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. (IJBMB1004002).
Keywords:
Full Text PDF
Address all correspondence to:
Guangbin Luo, PhD
Department of Genetics, School of Medicine
Case Western Reserve University
Biomedical Research Building 720
2109 Adelbert Road, Cleveland, OH 44106-4955, USA.
Tel: 1-(216)-368-4883; Fax: 1-(216)-368-3432
E-mail: guangbin.luo@case.edu
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