| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Animal: DNA Viruses |
Department of Medical Microbiology and Immunology, Texas A&M University System Health Science Center, College Station, TX 77843-1114, USA1
The Institute of Advanced Studies, John Curtin School of Medical Research, PO Box 334, Canberra City, ACT 2601, Australia2
Office of Texas State Chemist, MS 2114, Texas A&M University, College Station, TX 77843-2114, USA3
Author for correspondence: Van Wilson. Fax +1 979 845 3479. e-mail v-wilson{at}tamu.ed
The interaction between papillomavirus E1 and E2 proteins is essential for viral 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 E1, 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 E2BS12 was also examined, and cooperative binding was only observed when E2 was bound to E2BS12.
This article has been cited by other articles:
|
|
 |
|
  X.-L. Bian, G. Rosas-Acosta, Y.-C. Wu, and V. G. Wilson Nuclear Import of Bovine Papillomavirus Type 1 E1 Protein Is Mediated by Multiple Alpha Importins and Is Negatively Regulated by Phosphorylation near a Nuclear Localization Signal J. Virol., March 15, 2007; 81(6): 2899 - 2908. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Titolo, K. Brault, J. Majewski, P. W. White, and J. Archambault Characterization of the Minimal DNA Binding Domain of the Human Papillomavirus E1 Helicase: Fluorescence Anisotropy Studies and Characterization of a Dimerization-Defective Mutant Protein J. Virol., May 1, 2003; 77(9): 5178 - 5191. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Sheikh, G. Van Horn, A. Naqvi, L. Sheahan, and S. A. Khan Purification and biochemical characterization of the E1 replication initiation protein of the cutaneous human papillomavirus type 1 J. Gen. Virol., February 1, 2003; 84(2): 277 - 285. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. West, D. Flanery, K. Woytek, D. Rangasamy, and V. G. Wilson Functional Mapping of the DNA Binding Domain of Bovine Papillomavirus E1 Protein J. Virol., December 15, 2001; 75(24): 11948 - 11960. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
