Interactions between the full complement of human RNA polymerase II subunits.
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.
Schaller
S
S
Institut de Génétique et de Biologie Moléculaire et Cellulaire (CNRS/INSERM/ULP), BP 163, 67404, Illkirch, France.
Grandemange
S
S
Shpakovski
G V
GV
Golemis
E A
EA
Kedinger
C
C
Vigneron
M
M
D000818:Animals; D002460:Cell Line; D018076:DNA, Complementary / Q000235:genetics; D005816:Genetic Complementation Test; D006801:Humans; D017924:Nucleopolyhedroviruses / Q000235:genetics; D011487:Protein Conformation; D012319:RNA Polymerase II / Q000737:chemistry* / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000502:physiology; D018411:Spodoptera; D013696:Temperature
D018076:DNA, Complementary; D011993:Recombinant Fusion Proteins; D012319:RNA Polymerase II