有哪些信誉好的足球投注网站identification and developmental expression of xenopus laevis sumo proteases识别和发展表达非洲爪蟾蜍光滑的相扑蛋白酶.pdfVIP
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identification and developmental expression of xenopus laevis sumo proteases识别和发展表达非洲爪蟾蜍光滑的相扑蛋白酶
Identification and Developmental Expression of Xenopus laevis SUMO Proteases 1 1 1 1¤a 1 Yonggang Wang , Debaditya Mukhopadhyay , Smita Mathew , Takashi Hasebe , Rachel A. Heimeier , 1¤b 2 1 2 1 Yoshiaki Azuma , Nagamalleswari Kolli , Yun-Bo Shi , Keith D. Wilkinson , Mary Dasso * 1 Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, Bethesda, Maryland, United States of America, 2 Department of Biochemistry, Emory University, Atlanta, Georgia, United States of America Abstract SUMO proteins are small ubiquitin-related modifiers. All SUMOs are synthesized as propeptides that are post-translationally cleaved prior to conjugation. After processing, SUMOs become covalently conjugated to cellular targets through a pathway that is similar to ubiquitination. Ubiquitin like protein proteases/Sentrin specific proteases (Ulp/SENPs) mediate both processing and deconjugation of SUMOs. The action of Ulp/SENPs makes SUMOylation a highly dynamic post-translational modification. To investigate how Ulp/SENPs are regulated in a developmental context, we isolated and characterized all Ulp/SENPs in Xenopus laevis. Xenopus possess homologues of mammalian SENP3, 5, 6 and 7. All of these enzymes reacted with HA-tagged vinyl sulfone derivatives of SUMO-2 (HA-SU2-VS) but not SUMO-1 (HA-SU1-VS), suggesting that they act primarily on SUMO-2 and -3. In contrast, Xenopus possess a single member of the SENP1/SENP2 subfamily of Ulp/SENPs, most closely related to mammalian SENP1.
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