ADENOVIRUS DNA-POLYMERASE - DOMAIN ORGANIZATION AND INTERACTION WITH PRETERMINAL PROTEIN

Citation
Ej. Parker et al., ADENOVIRUS DNA-POLYMERASE - DOMAIN ORGANIZATION AND INTERACTION WITH PRETERMINAL PROTEIN, Nucleic acids research, 26(5), 1998, pp. 1240-1247
Citations number
50
Categorie Soggetti
Biology
Journal title
ISSN journal
03051048
Volume
26
Issue
5
Year of publication
1998
Pages
1240 - 1247
Database
ISI
SICI code
0305-1048(1998)26:5<1240:AD-DOA>2.0.ZU;2-8
Abstract
Adenovirus DNA polymerase is one of three viral proteins and two cellu lar proteins required for replication of the adenovirus genome. During initiation of viral DNA synthesis the viral DNA polymerase transfers dCMP onto the adenovirus preterminal protein, to which it is tightly b ound, The domain structure of the 140 kDa DNA polymerase has been prob ed by partial proteolysis and the sites of proteolytic cleavage determ ined by N-terminal sequencing, At least four domains can be recognised within the DNA polymerase, Adenovirus preterminal protein interacts w ith three of the four proteolytically derived domains, This was confir med by cloning and expression of each of the individual domains, These data indicate that, like other members of the pol alpha family of DNA polymerases, the adenovirus DNA polymerase has a multidomain structur e and that interaction with preterminal protein takes place with non-c ontiguous regions of the polypeptide chain over a large surface area o f the viral DNA polymerase.