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Titolo:
Effects of mutations within two hydrophilic regions of the bovine papillomavirus type 1 E1 DNA-binding domain on E1-E2 interaction
Autore:
Woytek, KJ; Rangasamy, D; Bazaldua-Hernandez, C; West, M; Wilson, VG;
Indirizzi:
Texas A&M Univ, Syst Hlth Sci Ctr, Dept Med Microbiol & Immunol, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 mmunol, College Stn, TX 77843 USA Australian Natl Univ, John Curtin Sch Med Res, Inst Adv Studies, Canberra,ACT 2601, Australia Australian Natl Univ Canberra ACT Australia 2601 erra,ACT 2601, Australia Texas A&M Univ, Off Texas State Chem, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 e Chem, College Stn, TX 77843 USA
Titolo Testata:
JOURNAL OF GENERAL VIROLOGY
, volume: 82, anno: 2001,
parte:, 10
pagine: 2341 - 2351
SICI:
0022-1317(200110)82:<2341:EOMWTH>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTIONAL ACTIVATOR E2; REPLICATION PROTEIN-A; COMPLEX-FORMATION; POLYMERASE-ALPHA; TERMINAL DOMAIN; INITIATOR E1; IN-VITRO; VIRAL E1; ORIGIN; HELICASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Wilson, VG Texas A&M Univ, Syst Hlth Sci Ctr, Dept Med Microbiol & Immunol, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 lege Stn, TX 77843 USA
Citazione:
K.J. Woytek et al., "Effects of mutations within two hydrophilic regions of the bovine papillomavirus type 1 E1 DNA-binding domain on E1-E2 interaction", J GEN VIROL, 82, 2001, pp. 2341-2351

Abstract

The interaction between papillomavirus E1 and E2 proteins is essential forviral genome replication. Using both in vivo and in vitro assays to evaluate the regions of the two proteins necessary for the E1-E2 interaction, three independent interactions were identified for bovine papillomavirus E1: the N terminus of E1 (E1N, residues 1-311) interacts with the E2 transactivation domain (E2TAD) and the E2 DNA-binding domain (E2DBD) and the C terminus of E1 (E1C, residues 315-605) interacts with E2. Nine mutations within E1N were evaluated for their effects on E2 interaction. Five mutations eliminated interaction with the E2TAD; four of these were located within two previously identified conserved, hydrophilic regions, HR1 and HR3. Since HR1 and HR3 residues appear to comprise the origin of replication recognition element for El, simultaneous interaction with the E2TAD during initiation complex formation would seem unlikely. Consistent with this inference is the fact that three of the five mutants defective for E2TAD binding exhibited wild-type levels of replication. The replication-positive phenotype of these mutants suggests that the E1N-E2TAD interaction is not essential for replication function and is probably involved in some other E1-E2 function, such as regulating transcription. Only one of the five mutations defective for E2TAD binding also prevented E2DBD interaction, indicating that the regions of E1N that interact with the E2TAD and the E2DBD are not identical. The ability of E1N to cooperatively interact with E2 bound to E2-binding site (E2BS) 11 versus EBS12 was also examined, and cooperative binding was only observed when E2 was bound to E2BS12.

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Documento generato il 27/09/20 alle ore 19:47:23