Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/147880
Title: Structural and biochemical study of Candida albicans polarisomal proteins AIP5 and SPA2
Authors: Loh, Zhi Yang
Keywords: Science::Biological sciences::Biochemistry
Science::Biological sciences::Microbiology
Issue Date: 2020
Publisher: Nanyang Technological University
Source: Loh, Z. Y. (2020). Structural and biochemical study of Candida albicans polarisomal proteins AIP5 and SPA2. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/147880
Abstract: The polarisome is a multi-protein complex involved in the assembly of actin cytoskeleton during polarised hyphae growth in pathogenic yeast C. albicans. In this thesis, we present the crystal structures of C. albicans polarisomal proteins Aip5 (786-896) and Spa2 (1309-1466) at 2.65 Å and 1.36 Å resolution, respectively. Structural comparison of nucleation promoting factor Aip5 with its S. cerevisiae homolog revealed the difference in actin-binding loop flexibility, which may account for their differential actin-binding affinities reported in literature. Spa2 is a putative scaffold protein of the polarisome. Its crystal structure revealed a tetra-helical bundle resembling coiled-coil proteins. Structural comparison with its homologs indicated that Spa2 inter-helical grooves might facilitate its association with other polarisomal proteins. We also report two potential Spa2 inhibitors capable of inhibiting hyphae growth in vivo. Together, the crystal structures of Aip5 and Spa2 provide insights into their roles in the polarisome complex and filamentous growth.
URI: https://hdl.handle.net/10356/147880
Rights: This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).
Fulltext Permission: embargo_20260414
Fulltext Availability: With Fulltext
Appears in Collections:SBS Theses

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