Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae

Polarisome, a fuzzy multiprotein complex, regulates polarized cell growth in both budding yeast and filamentous fungi through actin polymerization. Here we reported a previously uncharacterized gene YFR016C that encodes a novel fourth type of actin nucleation factor, named Aip5. Through X-ray crysta...

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Bibliographic Details
Main Author: Sun, Jialin
Other Authors: Gao Yonggui
Format: Thesis
Language:English
Published: 2018
Subjects:
Online Access:https://hdl.handle.net/10356/86103
http://hdl.handle.net/10220/46705
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author Sun, Jialin
author2 Gao Yonggui
author_facet Gao Yonggui
Sun, Jialin
author_sort Sun, Jialin
collection NTU
description Polarisome, a fuzzy multiprotein complex, regulates polarized cell growth in both budding yeast and filamentous fungi through actin polymerization. Here we reported a previously uncharacterized gene YFR016C that encodes a novel fourth type of actin nucleation factor, named Aip5. Through X-ray crystallography, we have unveiled the structure of Aip5 C-terminal domain (Aip5-C), which is the functional component for actin nucleation. Structural analysis of both the wild type and mutant Aip5-C revealed that Aip5-C directly interacts with G-actin via a loop region to nucleate actin filaments. Rubisco is the key enzyme for carbon fixation during photosynthesis. Owing to its sluggish enzymatic activity, Rubisco activase is required to modulate Rubisco’s activity. In the unicellular red algae Cyanidioschyzon merolae, there are two isoforms (plastid and nuclear) of the CbbX protein that complex to form a functional Rubisco activase. Through X-ray crystallography, we have determined the structure of CbbX plastid isoform. RuBP and ATP binding sites appeared to be conserved. However, more effort is required to improve the crystal diffraction of CbbX nuclear isoform and CbbX complex to elucidate its regulatory mechanism.
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spelling ntu-10356/861032023-02-28T18:47:08Z Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae Sun, Jialin Gao Yonggui School of Biological Sciences A*STAR Institute of Molecular and Cell Biology Hong Wanjin DRNTU::Science::Biological sciences Polarisome, a fuzzy multiprotein complex, regulates polarized cell growth in both budding yeast and filamentous fungi through actin polymerization. Here we reported a previously uncharacterized gene YFR016C that encodes a novel fourth type of actin nucleation factor, named Aip5. Through X-ray crystallography, we have unveiled the structure of Aip5 C-terminal domain (Aip5-C), which is the functional component for actin nucleation. Structural analysis of both the wild type and mutant Aip5-C revealed that Aip5-C directly interacts with G-actin via a loop region to nucleate actin filaments. Rubisco is the key enzyme for carbon fixation during photosynthesis. Owing to its sluggish enzymatic activity, Rubisco activase is required to modulate Rubisco’s activity. In the unicellular red algae Cyanidioschyzon merolae, there are two isoforms (plastid and nuclear) of the CbbX protein that complex to form a functional Rubisco activase. Through X-ray crystallography, we have determined the structure of CbbX plastid isoform. RuBP and ATP binding sites appeared to be conserved. However, more effort is required to improve the crystal diffraction of CbbX nuclear isoform and CbbX complex to elucidate its regulatory mechanism. Doctor of Philosophy 2018-11-26T07:32:14Z 2019-12-06T16:16:07Z 2018-11-26T07:32:14Z 2019-12-06T16:16:07Z 2018 Thesis Sun, J. (2018). Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/86103 http://hdl.handle.net/10220/46705 10.32657/10220/46705 en 137 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences
Sun, Jialin
Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae
title Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae
title_full Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae
title_fullStr Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae
title_full_unstemmed Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae
title_short Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae
title_sort structural and functional studies of 1 actin interacting protein 5 a novel actin assembly regulator in saccharomyces cerevisiae 2 cbbx a red type rubisco activase in cyanidioschyzon merolae
topic DRNTU::Science::Biological sciences
url https://hdl.handle.net/10356/86103
http://hdl.handle.net/10220/46705
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