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Characterization of a Dual-Specificity Protein Phosphatase, Human DUSP28
Dae Gwin Jeong(정대균),Song Yi Kim(김송이),Jeong Hun Yun(윤정훈),Jae Hoon Kim(김재훈) 한국생명과학회 2011 생명과학회지 Vol.21 No.1
Dual-specificity protein phosphatase (DUSP)들은 인산화된 티로신 잔기와 인산화된 세린 또는 트레오닌 잔기를 탈인산화시키는 단백질 탈인산화효소 군을 이루고 있으며, 대부분의 DUSP들은 세포의 생존이나 분화에 관여하고 있다. 본 연구에서는 잘 알려지지 않은 인간 유래의 dual-specificity protein phosphatase인 DUSP28을 인간신장 cDNA에서 분리하였다. 대장균에서 생산된 재조합단백질은 6,8-difluoro-4-methylumbelliferyl phosphate(DiFMUP)에 대하여 좋은 활성을 보였다. 다양한 저해제와 2가 금속이온들이 DUSP28의 활성에 미치는 영향을 조사하였다. 다른 DUSP들에서와는 다르게, Zn<SUP>2+</SUP>은 DUSP28의 탈인산화활성을 강하게 억제하였다. 이러한 결과로부터 DUSP28이 Zn과 연관된 신호전달경로에 관여할 것으로 추정된다. 더욱이, DUSP28은 인산화된 티로신 잔기를 더욱 선호하는 경향이 있는 것으로 나타났고, 이는 세포 내에서도 비슷한 작용을 할 것으로 예상된다. Dual-specificity protein phosphatases (DUSPs) constitute a family of protein phosphatase characterized by the ability to dephosphorylate phospho-tyrosyl and phospho-seryl/threonyl residues. Most DUSPs are involved in regulation of cell survival and differentiation. In this study, a human dual-specificity protein phosphatase, DUSP28, was isolated from a human kidney cDNA. The recombinant protein was successfully produed in E.coli and showed sufficient phosphatase activity toward DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate). Various phosphatase inhibitors and divalent metals were tested for their effects on the DUSP28 phosphatase activity. As a result, Zn<SUP>2+</SUP> was found to strongly inhibit DUSP28 phosphatase activity, suggesting DUSP28 is involved in Zn-related signal transduction pathway. Furthermore, the DUSP28 protein preferred phospho-tyrosyl residues to phospho-threonyl residues, implying its physiological roles in the cellular process.
( Jeong Ki Kim ),( Jeong Hyun Nam ),( Kwang Soo Lyoo ),( Hyoungjoon Moon ),( Woonsung Na ),( Eun Jung Song ),( Minjoo Yeom ),( Sang Mu Shim ),( Dae Gwin Jeong ),( Dong Jun An ),( Bo Kyu Kang ),( Daesu 한국미생물 · 생명공학회 2016 Journal of microbiology and biotechnology Vol.26 No.6
H3N2 canine influenza virus emerged in South Korea in 2007 and subsequently spread to China and Thailand, causing epidemic or endemic respiratory diseases in dogs. Through intermammalian species transmission, the virus has also infected cats. However, no direct evidence of significant genetic evolution has been reported since its first emergence. Here, we describe in depth the genetic and molecular characteristics of the ancestral strain (i.e., the first virus isolate from South Korea) of the H3N2 canine influenza virus currently circulating in East Asia.
Krishnan, Navasona,Jeong, Dae Gwin,Jung, Suk-Kyeong,Ryu, Seong Eon,Xiao, Andrew,Allis, C David,Kim, Seung Jun,Tonks, Nicholas K American Society for Biochemistry and Molecular Bi 2009 The Journal of biological chemistry Vol.284 No.24
<P>In mammalian cells, the DNA damage-related histone H2A variant H2A.X is characterized by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an atypical kinase, WSTF. The phosphorylation status of Tyr-142 in H2A.X has been shown to be an important regulator of the DNA damage response by controlling the formation of gammaH2A.X foci, which are platforms for recruiting molecules involved in DNA damage repair and signaling. In this work, we present evidence to support the identification of the Eyes Absent (EYA) phosphatases, protein-tyrosine phosphatases of the haloacid dehalogenase superfamily, as being responsible for dephosphorylating the C-terminal tyrosyl residue of histone H2A.X. We demonstrate that EYA2 and EYA3 displayed specificity for Tyr-142 of H2A.X in assays in vitro. Suppression of eya3 by RNA interference resulted in elevated basal phosphorylation and inhibited DNA damage-induced dephosphorylation of Tyr-142 of H2A.X in vivo. This study provides the first indication of a physiological substrate for the EYA phosphatases and suggests a novel role for these enzymes in regulation of the DNA damage response.</P>