RecQ-like DNA helicase BLM

Definition:

ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction. Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity).

References:

[1]. J K Karow, et al. The Bloom's syndrome gene product is a 3'-5' DNA helicase. J Biol Chem. 1997 Dec 5;272(49):30611-4. [Content Brief]

[2]. Sun-Yong Kim, et al. Structure of the RecQ C-terminal domain of human Bloom syndrome protein. Sci Rep. 2013 Nov 21;3:3294. [Content Brief]

[3]. Gregory Langland, et al. The BLM helicase is necessary for normal DNA double-strand break repair. Cancer Res. 2002 May 15;62(10):2766-70. [Content Brief]

[4]. Young Mee Kim, et al. Structure and function of the regulatory HRDC domain from human Bloom syndrome protein. Nucleic Acids Res. 2010 Nov;38(21):7764-77. [Content Brief]

[5]. Michael K Swan, et al. Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNA. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1465-75. [Content Brief]

[6]. Amitabh V Nimonkar, et al. BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev. 2011 Feb 15;25(4):350-62. [Content Brief]

[7]. Li Wan, et al. Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair. Proc Natl Acad Sci U S A. 2013 Jun 25;110(26):10646-51. [Content Brief]

[8]. Joseph A Newman, et al. Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Res. 2015 May 26;43(10):5221-35. [Content Brief]

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