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Histone acetyltransferase p300/CBP‐associated factor is an effective suppressor of secretory immunoglobulin synthesis in immature B cells
Author(s) -
Kikuchi Hidehiko,
Nakayama Masami,
Kawai Chikage,
Kuribayashi Futoshi,
Mimuro Hitomi,
ImajohOhmi Shinobu,
Nishitoh Hideki,
Takami Yasunari,
Nakayama Tatsuo
Publication year - 2015
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/1348-0421.12237
Subject(s) - pcaf , histone , histone acetyltransferase , biology , j chain , acetyltransferase , acetylation , immunoglobulin light chain , chromatin , antibody , microbiology and biotechnology , gene , biochemistry , immunology
The histone acetyltransferase p300/CBP‐associated factor (PCAF) catalyzes acetylation of core histones and plays important roles in epigenetics by altering the chromatin structure in vertebrates. In this study, PCAF‐deficient DT40 mutants were analyzed and it was found that PCAF participates in regulation of secretory IgM heavy chain (H‐chain) synthesis. Remarkably, PCAF‐deficiency causes an increase in the amount of secretory IgM H‐chain mRNA, but not in that of IgM light chain and membrane‐bound IgM H‐chain mRNAs, resulting in dramatic up‐regulation of the amount of secretory IgM protein. These findings suggest that PCAF regulates soluble antibody production and is thus an effective suppressor of secretory IgM H‐chain synthesis.