TAILIEUCHUNG - Báo cáo khoa học: Sumoylation of a meiosis-specific RecA homolog, Lim15/Dmc1, via interaction with the small ubiquitinrelated modifier (SUMO)-conjugating enzyme Ubc9

Sumoylation is a post-translational modification system that covalently attaches the small ubiquitin-related modifier (SUMO) to target proteins. Ubc9 is required as the E2-type enzyme for SUMO-1 conjugation to tar-gets. Here, we show that Ubc9 interacts with the meiosis-specific RecA homolog, Lim15⁄Dmc1 in the basidiomyceteCoprinus cinereus(CcLim15), and mediates sumoylation of CcLim15 during meiosis. | ỊFEBS Journal Sumoylation of a meiosis-specific RecA homolog Lim15 Dmc1 via interaction with the small ubiquitin-related modifier SUMO -conjugating enzyme Ubc9 Akiyo Koshiyama Fumika N. Hamada Satoshi H. Namekawa Kazuki Iwabata Hiroko Sugawara Aiko Sakamoto Takashi Ishizaki and Kengo Sakaguchi Department of Applied BiologicalScience Tokyo University of Science Chiba-ken Japan Keywords sumoylation RecA meiotic recombination Coprinus cinereus post-translational modification Correspondence K. Sakaguchi Department of Applied BiologicalScience Tokyo University of Science 2641 Yamazaki Noda-shi Chiba-ken 278-8510 Japan Fax 81 471 23 9767 Tel. 81 471 24 1501 ext. 3409 E-mail kengo@ Received 25 April2006 revised 29 June 2006 accepted 3 July 2006 doi Sumoylation is a post-translational modification system that covalently attaches the small ubiquitin-related modifier SUMO to target proteins. Ubc9 is required as the E2-type enzyme for SUMO-1 conjugation to targets. Here we show that Ubc9 interacts with the meiosis-specific RecA homolog Lim15 Dmc1 in the basidiomycete Coprinus cinereus CcLim15 and mediates sumoylation of CcLim15 during meiosis. In vitro protein-protein interaction assays revealed that CcUbc9 interacts with CcLim15 and binds to the C-terminus amino acids 105-347 of CcLim15 which includes the ATPase domain. Immunocytochemistry demonstrates that CcUbc9 and CcLim15 colocalize in the nuclei from the leptotene stage to the early pachytene stage during meiotic prophase I. Coimmunoprecipitation experiments indicate that CcUbc9 interacts with CcLim15 in vivo during meiotic prophase I. Furthermore we show that CcLim15 is a target protein of sumoy-lation both in vivo and in vitro and identify the C-terminus amino acids 105-347 of CcLim15 as the site of sumoylation in vitro. These results suggest that sumoylation is a candidate modulator of meiotic recombination via interaction between Ubc9 and Lim15 Dmc1. Sumoylation is .

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