A cytoplasmic coiled-coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1

作者: Wei Tao , Cheryl L. Malone , Addison D. Ault , Robert J. Deschenes , Jan S. Fassler

DOI: 10.1046/J.1365-2958.2002.02757.X

关键词: MAP kinase kinase kinaseBiologyCell biologyBiochemistryMitogen-activated protein kinase kinaseHistidine kinaseASK1Cyclin-dependent kinase 9Cyclin-dependent kinase 2Kinase activityMAP2K7

摘要: Summary The yeast histidine kinase, Sln1p, is a plasma membrane-associated osmosensor that regulates the activity of osmotic stress MAP kinase pathway. Changes in environment cell influence autokinase cytoplasmic domain Sln1p. Neither nature stimulus, mechanism by which signal transduced nor manner regulated currently clear. We have identified several mutations located linker region Sln1 (just upstream domain) cause hyperactivity kinase. This kinases largely uncharacterized, but its location between transmembrane domains and suggests it may potential role transduction. In this study, we investigated order to understand function transduction regulation activity. Our results indicate forms coiled-coil structure suggest alterations induced altering alignment phospho-accepting with respect catalytic

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