ppat.1011978.s013.tif (339.22 kB)
SRPK1 does not phosphorylate T162 in vitro.
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posted on 2024-02-07, 18:40 authored by Ryan Pak Hong YIP, Doris Ching Ying Kwok, Louis Tung Faat Lai, Siu-Ming Ho, Ivan Chun Kit Wong, Chi-Ping Chan, Wilson Chun Yu Lau, Jacky Chi Ki NgoIn vitro radioactive kinase assay was performed using SRPK1WT and the mutational Cp constructs, with six/seven alanine substitution at the phosphorylatable sites, in the presence of [32P]ATP. Reactions were quenched after 10 mins and analyzed by SDS-PAGE. The gel was visualized with Coomassie Blue staining and then subjected to autoradiography. Mutation of six serines to alanines abolished the phosphorylation of Cp by SRPK1.
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pregenomic rna encapsidationelectron microscopy structureviral protein reactivatedviral nucleocapsid assemblyimportant cellular kinaseregulating capsid assemblyidentified cp sitesdiv >< pspecific docking grooveviral capsiddocking groovekinase utilizeshbv capsiddocking interactionvitro terminal domainpregenome packagingnew cryokinases decoratedirect interactionassays together>, whereas
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