The gene (POLR2L) encoding a 7.6-kDa subunit (hRPB7.6) of human RNA po
lymerase has been cloned. It comprises two exons, 116 and 227 bp, resp
ectively, interspaced with an intron of about 2.1 kb. This gene, whose
localization has been assigned to the short arm of chromosome 11 (pos
ition 11p15), is transcribed in HeLa cells as one major messenger RNA,
which encodes a 67-residue polypeptide (7645 La) that shares strong h
omologies with the corresponding subunits of other eukaryotic and arch
aeal RNA polymerase subunits. Like its yeast counterpart (ABC10 beta,
encoded by the RPB10 gene), the hRPB7.6 subunit may be shared by all t
hree classes of human nuclear RNA polymerase. Cysteine residues charac
teristic of an atypical zinc-binding domain are conserved in the homol
ogous sequences of all six species analyzed. A small, related RNA poly
merase subunit from vaccinia virus exhibits an identical set of cystei
nes, suggesting that these residues may contribute to a crucial functi
on in the multimeric RNA polymerases. (C) 1996 Academic Press, Inc.