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Proteolytic cleavage of ALF into α‐ and β‐subunits that form homologous and heterologous complexes with somatic TFIIA and TRF2 in male germ cells
Author(s) -
Catena Raffaella,
Argentini Manuela,
Martianov Igor,
Parello Catherine,
Brancorsini Stefano,
Parvinen Martti,
Sassone-Corsi Paolo,
Davidson Irwin
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.083
Subject(s) - somatic cell , biology , cleavage (geology) , homologous recombination , microbiology and biotechnology , heterologous , homologous chromosome , transcription factor ii a , transcription (linguistics) , genetics , gene , promoter , gene expression , paleontology , linguistics , philosophy , fracture (geology)
Male germ cells specifically express paralogues of components of the general transcription apparatus including ALF a paralogue of TFIIAα/β. We show that endogenous ALF is proteolytically cleaved to give α‐ and β‐subunits and we map the proteolytic cleavage site by mass spectrometry. Immunoprecipitations show that ALFα‐ and β‐subunits form a series of homologous and heterologous complexes with somatic TFIIA which is coexpressed in male germ cells. In addition, we show that ALF is coexpressed in late pachytene spermatocytes and in haploid round spermatids with transcription factor TRF2, and that these proteins form stable complexes in testis extracts. Our observations highlight how cleavage of ALF and coexpression with TFIIA and TRF2 increases the combinatorial possibilities for gene regulation at different developmental stages of spermatogenesis.