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Regulated expression of the ubiquitin protein ligase, E3 Histone /LASU1/Mule/ARF‐BP1/HUWE1, during spermatogenesis
Author(s) -
Liu Zhiqian,
Miao Dengsheng,
Xia Qingwen,
Hermo Louis,
Wing Simon S.
Publication year - 2007
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/dvdy.21302
Subject(s) - ubiquitin ligase , biology , histone , chromatin , spermatogenesis , ubiquitin , chromatin immunoprecipitation , histone h2a , histone h1 , microbiology and biotechnology , histone h4 , gene expression , genetics , endocrinology , gene , promoter
A ubiquitin protein ligase (E3), E3 Histone /LASU1 (Mule/ARF‐BP1/HUWE1), was recently identified that mediates ubiquitination of core histones, the Mcl‐1 anti‐apoptotic protein, and the p53 tumor suppressor protein. However, the expression of E3 Histone /LASU1 remains poorly studied. Because we identified E3 Histone /LASU1 from the testis, we explored its regulation during spermatogenesis. In the first wave of rat spermatogenesis, E3 Histone /LASU1 mRNA and protein had peak expression at days 10 and 20, respectively, and decreased with age. Consistent with these findings, immunohistochemistry revealed that E3 Histone /LASU1 was highly expressed in nuclei from spermatogonia to mid‐pachytene spermatocytes. There was no obvious staining in spermatids, when histones are ubiquitinated and degraded. E3 Histone /LASU1 was also expressed in other tissues. However, except in neuronal cells of the brain, expression was cytoplasmic. Thus, E3 Histone /LASU1 may play a role in chromatin modification in early germ cells of the testis, but also has functions in other tissues. Developmental Dynamics 236:2889–2898, 2007. © 2007 Wiley‐Liss, Inc.