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Interactions between the full complement of human RNA polymerase II subunits
Author(s) -
Schaller Sophie,
Grandemange Sylvie,
Shpakovski George V.,
Golemis Erica A.,
Kedinger Claude,
Vigneron Marc
Publication year - 1999
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/s0014-5793(99)01441-6
Subject(s) - protein subunit , complementation , polymerase , rna polymerase , complement (music) , yeast , protein fragment complementation assay , biology , transcription factor ii d , genetics , rna , chemistry , gene , phenotype
As an approach to elucidating the rules governing the assembly of human RNA polymerase II (hRPB), interactions between its subunits have been systematically analyzed. Eleven of the 12 expected hRPB subunits have previously been tested for reciprocal interactions (J. Biol. Chem. 272 (1997) 16815–16821). We now report the results obtained for the last subunit (hRPB4; Mol. Cell. Biol. 18 (1998) 1935–1945) and propose an essentially complete picture of the potential interactions occurring within hRPB. Finally, complementation experiments in yeast indicated that hRPB4 expression efficiently cured both heat and cold‐sensitivity of RPB4‐lacking strains, supporting the existence of conserved functional subunit interactions.