Liu, X., Stenlund, A. (February 2010) Mutations in Sensor 1 and Walker B in the bovine papillomavirus E1 initiator protein mimic the nucleotide bound state. Journal of Virology, 84 (4). pp. 1912-1919. ISSN 0022-538X
Abstract
Viral replication initiator proteins are multifunctional proteins that utilize ATP binding and hydrolysis by their AAA+ modules for multiple functions in the replication of their viral genomes. These proteins are therefore of particular interest for understanding how AAA+ proteins carry out multiple ATP driven functions. We have performed a comprehensive mutational analysis of the residues involved in ATP binding and hydrolysis in the papillomavirus E1 initiator protein based on the recent structural data. Ten of the 11 residues that were targeted were defective for ATP hydrolysis and seven of these were also defective for ATP binding. The three mutants that could still bind nucleotide represent the Walker B motif (D478, D479) and Sensor 1 (N523), three residues that are in close proximity to each other and generally are considered to be involved in ATP hydrolysis. Surprisingly however, two of these mutants, D478A and N523A, mimicked the nucleotide bound state and were capable of binding DNA in the absence of nucleotide. However, these mutants could not form the E1 double trimer (DT) in the absence of nucleotide, demonstrating that there are two qualitatively different consequences of ATP binding by E1, one which can be mimicked by D478A and N523A and one which cannot.
| Item Type: | Paper |
|---|---|
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication organism description > virus > papillomavirus |
| CSHL Authors: | |
| Communities: | CSHL labs > Stenlund lab CSHL Cancer Center Shared Resources > DNA Sequencing Service |
| Depositing User: | Brian Soldo |
| Date: | 25 February 2010 |
| Date Deposited: | 14 Mar 2012 15:37 |
| Last Modified: | 30 Dec 2014 16:22 |
| PMCID: | PMC2812389 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/25175 |
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