Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP

Bacterial polynucleotide phosphorylase (PNPase) is a 3'-5' processive exoribonuclease that participates in mRNA turnover and quality control of rRNA precursors in many bacterial species. It also associates with the RNase E scaffold and other components to form a multi-enzyme RNA degradasom...

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Main Authors: Wang, Yu-Chuan, Chin, Ko-Hsin, Chuah, Mary Lay-Cheng, Liang, Zhao-Xun, Chou, Shan-Ho
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2013
Online Access:https://hdl.handle.net/10356/95330
http://hdl.handle.net/10220/9278
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-953302023-02-28T17:01:16Z Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP Wang, Yu-Chuan Chin, Ko-Hsin Chuah, Mary Lay-Cheng Liang, Zhao-Xun Chou, Shan-Ho School of Biological Sciences Bacterial polynucleotide phosphorylase (PNPase) is a 3'-5' processive exoribonuclease that participates in mRNA turnover and quality control of rRNA precursors in many bacterial species. It also associates with the RNase E scaffold and other components to form a multi-enzyme RNA degradasome machinery that performs a wider regulatory role in degradation, quality control and maturation of mRNA and noncoding RNA. Several crystal structures of bacterial PNPases, as well as some biological activity studies, have been published. However, how the enzymatic activity of PNPase is regulated is less well understood. Recently, Escherichia coli PNPase was found to be a direct c-di-GMP binding target, raising the possibility that c-di-GMP may participate in the regulation of RNA processing. Here, the successful cloning, purification and crystallization of S1-domain-truncated Xanthomonas campestris PNPase (XcPNPaseΔS1) in the presence of c-di-GMP are reported. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 132.76, b = 128.38, c = 133.01 Å, γ = 93.3°, and diffracted to a resolution of 2.00 Å. Published version 2013-02-27T04:39:00Z 2019-12-06T19:12:43Z 2013-02-27T04:39:00Z 2019-12-06T19:12:43Z 2012 2012 Journal Article Wang, Y.- C., Chin, K.- H., Chuah, M. L.- C., Liang, Z.- X., & Chou, S.- H. (2012). Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(10), 1247-1250. 1744-3091 https://hdl.handle.net/10356/95330 http://hdl.handle.net/10220/9278 10.1107/S1744309112036202 23027759 en Acta Crystallographica Section F Structural Biology and Crystallization Communications © 2012 International Union of Crystallography. This paper was published in Acta Crystallographica Section F Structural Biology and Crystallization Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S1744309112036202]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
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language English
description Bacterial polynucleotide phosphorylase (PNPase) is a 3'-5' processive exoribonuclease that participates in mRNA turnover and quality control of rRNA precursors in many bacterial species. It also associates with the RNase E scaffold and other components to form a multi-enzyme RNA degradasome machinery that performs a wider regulatory role in degradation, quality control and maturation of mRNA and noncoding RNA. Several crystal structures of bacterial PNPases, as well as some biological activity studies, have been published. However, how the enzymatic activity of PNPase is regulated is less well understood. Recently, Escherichia coli PNPase was found to be a direct c-di-GMP binding target, raising the possibility that c-di-GMP may participate in the regulation of RNA processing. Here, the successful cloning, purification and crystallization of S1-domain-truncated Xanthomonas campestris PNPase (XcPNPaseΔS1) in the presence of c-di-GMP are reported. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 132.76, b = 128.38, c = 133.01 Å, γ = 93.3°, and diffracted to a resolution of 2.00 Å.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Wang, Yu-Chuan
Chin, Ko-Hsin
Chuah, Mary Lay-Cheng
Liang, Zhao-Xun
Chou, Shan-Ho
format Article
author Wang, Yu-Chuan
Chin, Ko-Hsin
Chuah, Mary Lay-Cheng
Liang, Zhao-Xun
Chou, Shan-Ho
spellingShingle Wang, Yu-Chuan
Chin, Ko-Hsin
Chuah, Mary Lay-Cheng
Liang, Zhao-Xun
Chou, Shan-Ho
Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
author_sort Wang, Yu-Chuan
title Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
title_short Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
title_full Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
title_fullStr Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
title_full_unstemmed Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP
title_sort crystallization and preliminary x-ray diffraction studies of xanthomonas campestris pnpase in the presence of c-di-gmp
publishDate 2013
url https://hdl.handle.net/10356/95330
http://hdl.handle.net/10220/9278
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