The Rex proteins of human T-cell leukemia virus type II differ by serine phosphorylation | Zendy

P L Green | Zendy; Yiming Xie | Zendy; I S Chen | Zendy

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The Rex proteins of human T-cell leukemia virus type II differ by serine phosphorylation

Author(s) -

P L Green,

Yiming Xie,

I S Chen

Publication year - 1991

Publication title -

journal of virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.617

H-Index - 292

eISSN - 1070-6321

pISSN - 0022-538X

DOI - 10.1128/jvi.65.1.546-550.1991

Subject(s) - biology , serine , phosphorylation , microbiology and biotechnology , virus , cytoplasm , amino acid , human t lymphotropic virus 1 , gene , messenger rna , virology , gene expression , leukemia , biochemistry , genetics , t cell leukemia

The Rex proteins of human T-cell leukemia virus types I and II (HTLV-I and HTLV-II) induce cytoplasmic expression of unspliced gag-pol mRNA and singly spliced env mRNA and are critical for virus replication. Two rex gene products, p27rex and p21rex of HTLV-I and p26rex and p24rex of HTLV-II, have been detected in HTLV-infected cells; however, the structural and biological relationship of the proteins has not been clearly elucidated. Endoproteinase digestion and phosphoamino acid analysis of HTLV-II Rex indicated that p24rex has the same amino acid backbone as p26rex and that the larger apparent molecular size of p26rex is attributable to serine phosphorylation.

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