Tripathi, Ranjana and Kaithwas, Vikas and Dureja, Chetna and Raychaudhuri, Saumya (2013) Alanine-scanning mutagenesis of WH2 domains of VopF reveals residues important for conferring lethality in a Saccharomyces cerevisiae model. Gene, 525 (1). pp. 116-23. ISSN 1879-0038
Full text not available from this repository. (Request a copy)Abstract
VopF, the type III effector molecule, has been implicated in the pathogenesis of non-O1, non-O139 strains of Vibrio cholerae. It is a protein of 530 amino acids, comprises of one formin homology 1-like (FH1-like) domain and three WASP homology 2 (WH2) domains. Previous works have demonstrated that WH2 domains are crucial for VopF function as a modulator of cellular actin homeostasis. Furthermore, domain deletion analysis also suggests that VopF variant constituted with only WH2 domain 3 is more efficient in restricting the growth of budding yeast than its congeners containing either only domain 1 or domain 2. Interestingly, a good degree of sequence diversity is present within each WH2 domain of VopF. In order to ascertain the importance of different amino acids in each WH2 domain, a systemic alanine scanning mutagenesis was employed. Using a yeast model system, the alanine derivatives of each amino acid of WH2 domain 1 and 3 of VopF were examined for growth restricting activity. Taken together, our mutagenesis results reveal the identification of critical residues of WH2 domain 1 and 3 of VopF.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Elsevier. |
| Uncontrolled Keywords: | ype III effector proteinVibrio cholerae |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 19 Sep 2018 08:22 |
| Last Modified: | 19 Sep 2018 08:22 |
| URI: | http://crdd.osdd.net/open/id/eprint/2118 |
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