Abstract:
:Phosphorylated sites of calf thymus H2B histone were investigated with a catalytic fragment of 72 kDa protein-tyrosine kinase (p72syk). Three of five tyrosine residues in H2B histone can be phosphorylated by this kinase. In this analysis, H2B histone was thoroughly phosphorylated in vitro with [gamma-32P]ATP and the kinase, and then digested with a lysylendopeptidase. The resulting radioactive phosphopeptides were separated by a reverse-phase column on high performance liquid chromatography. Subsequent sequential Edman degradation of the purified phosphopeptides revealed that 40Y, 83Y and 121Y were phosphorylated. 121Y is the major phosphorylated residue in H2B histone. No phosphorylation was detected in 37Y and 42Y. Although the consensus sequence was not defined from these analyses, our data suggest that higher-order structure(s) in addition to primary one may participate in recognition of H2B histone by this protein kinase.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sakai K,Tanaka Y,Asahi M,Shimomura R,Taniguchi T,Hashimoto E,Yamamura Hdoi
10.1016/0014-5793(91)81352-9subject
Has Abstractpub_date
1991-12-02 00:00:00pages
104-8issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(91)81352-9journal_volume
294pub_type
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