ppat.1011978.s010.tif (744.1 kB)
SRPK1 and SRPK2 do not have additive effect on CpWT capsid phosphorylation.
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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 Ngo(A) Purification of His-CpWT. His-CpWT were purified using Ni-NTA affinity chromatography in the presence 6M urea. Samples were resolved by SDS-PAGE. (B) GuHCl was removed by dialysis to allow His-CpWT to assemble into capsids. The capsids were further purified by gel filtration. Protein collected from the peak fractions was analyzed by SDS-PAGE. (C) In vitro radioactive kinase assay was performed using the CpWT capids in the presence of SRPK1WT or SRPK2WT or both kinases. Samples were analyzed by SDS-PAGE and autoradiography. Presence of both SRPK1 and SRPK2 did not result in more phosphorylated Cp product.
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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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