Nucleic Acids Research, Vol 26, Issue 7 1700-1706, Copyright © 1998 by Oxford University Press
T Yamada-Okabe, R Doi, O Shimmi, M Arisawa and H Yamada-Okabe
The human mRNA 5'-capping enzyme cDNA was identified. Three highly related
cDNAs, HCE1 (human mRNAcappingenzyme1), HCE1A and HCE1B , were isolated
from a HeLa cDNA library. The HCE1 cDNA has the longest ORF, which can
encode a 69 kDa protein. A short region of 69 bp in the 3'- half of the
HCE1 ORF was missing in HCE1A and HCE1B , and, additionally, HCE1B has an
early translation termination signal, which suggests that the latter two
cDNAs represent alternatively spliced product. When expressed in
Escherichia coli as a fusion protein with glutathione S -transferase, Hce1p
displayed both mRNA 5'-triphosphatase (TPase) and mRNA
5'-guanylyltransferase (GTase) activities, and it formed a cap structure at
the 5'-triphosphate end of RNA, demonstrating that it indeed specifies an
active mRNA 5'-capping enzyme. The recombinant proteins derived from HCE1A
and HCE1B possessed only TPase activity. When expressed from ADH1 promoter,
HCE1 but not HCE1A and HCE1B complemented Saccharomyces cerevisiae CEG1 and
CET1 , the genes for GTase and TPase, respectively. These results
demonstrate that the N- terminal part of Hce1p is responsible for TPase
activity and the C- terminal part is essential for GTase activity. In
addition, the human TPase domain cannot functionally substitute for the
yeast enzyme in vivo.
ARTICLES
Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme
Department of Hygiene, School of Medicine, Yokohama City University, 3- 9, Fukuura, Kanazawa, Yokohama 236, Japan.
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