Primary structure of the second largest subunit of human RNA polymerase II (or B).
The cDNA of the second largest subunit of RNA polymerase II (or B) from HeLa cells has been cloned and sequenced. A predicted amino acid sequence of 1174 residues (calculated molecular mass of 133,896 Da) was derived from the longest open reading frame and compared to the sequences of homologous subunits of polymerases of eukaryotic, archaeal and bacterial origin. After optimal alignment, about 16% of the residues were found to be conserved throughout evolution, from human to Escherichia coli. About 2/3 of the overall length of the conserved domains delineated by these residues are clustered within the C-terminal half of the human polypeptide, whereas the remaining is spread over its N-terminal half. The putative functional significance of these conserved domains is discussed.
Acker
J
J
Laboratoire de Génétique Moléculaire des Eucaryotes (CNRS) Unité 184 de Biologie Moléculaire et de Génie Génétique (INSERM), Strasbourg, France.
Wintzerith
M
M
Vigneron
M
M
Kédinger
C
C
D000595:Amino Acid Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D012319:RNA Polymerase II / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid
D012319:RNA Polymerase II