Literature DB >> 28570540

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG.

Meong Il Kim1, Choongdeok Lee1, Minsun Hong2.   

Abstract

To overcome safety restrictions and regulations when studying genes and proteins from true pathogens, their homologues can be studied. Bacillus anthracis is an obligate pathogen that causes fatal inhalational anthrax. Bacillus cereus is considered a useful model for studying B. anthracis due to its close evolutionary relationship. The gene cluster ba1554 - ba1558 of B. anthracis is highly conserved with the bc1531- bc1535 cluster in B. cereus, as well as with the bt1364-bt1368 cluster in Bacillus thuringiensis, indicating the critical role of the associated genes in the Bacillus genus. This manuscript describes methods to prepare and characterize a protein product of the first gene (ba1554) from the gene cluster in B. anthracis using a recombinant protein of its ortholog in B. cereus, bc1531.

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Year:  2017        PMID: 28570540      PMCID: PMC5607965          DOI: 10.3791/55576

Source DB:  PubMed          Journal:  J Vis Exp        ISSN: 1940-087X            Impact factor:   1.355


  12 in total

1.  MazG -- a regulator of programmed cell death in Escherichia coli.

Authors:  Miryam Gross; Irina Marianovsky; Gad Glaser
Journal:  Mol Microbiol       Date:  2006-01       Impact factor: 3.501

2.  Protein production and crystallization at the joint center for structural genomics.

Authors:  Scott A Lesley; Ian A Wilson
Journal:  J Struct Funct Genomics       Date:  2005

3.  A putative house-cleaning enzyme encoded within an integron array: 1.8 A crystal structure defines a new MazG subtype.

Authors:  Andrew Robinson; Amy P Guilfoyle; Stephen J Harrop; Yan Boucher; H W Stokes; Paul M G Curmi; Bridget C Mabbutt
Journal:  Mol Microbiol       Date:  2007-09-24       Impact factor: 3.501

4.  Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase.

Authors:  Meong Il Kim; Minsun Hong
Journal:  Biochem Biophys Res Commun       Date:  2016-02-23       Impact factor: 3.575

5.  LmbE proteins from Bacillus cereus are de-N-acetylases with broad substrate specificity and are highly similar to proteins in Bacillus anthracis.

Authors:  Alexandra Deli; Dimitrios Koutsioulis; Vasiliki E Fadouloglou; Panagiota Spiliotopoulou; Stavroula Balomenou; Sofia Arnaouteli; Maria Tzanodaskalaki; Konstantinos Mavromatis; Michalis Kokkinidis; Vassilis Bouriotis
Journal:  FEBS J       Date:  2010-05-19       Impact factor: 5.542

Review 6.  Bacillus anthracis.

Authors:  R C Spencer
Journal:  J Clin Pathol       Date:  2003-03       Impact factor: 3.411

7.  Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-alpha NTP pyrophosphohydrolases with potential "house-cleaning" functions.

Authors:  Olga V Moroz; Alexey G Murzin; Kira S Makarova; Eugene V Koonin; Keith S Wilson; Michael Y Galperin
Journal:  J Mol Biol       Date:  2005-01-27       Impact factor: 5.469

8.  Structural and biochemical characterization of bacterial YpgQ protein reveals a metal-dependent nucleotide pyrophosphohydrolase.

Authors:  Ye Ji Jeon; Sun Cheol Park; Wan Seok Song; Ok-Hee Kim; Byung-Chul Oh; Sung-Il Yoon
Journal:  J Struct Biol       Date:  2016-04-07       Impact factor: 2.867

9.  The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases.

Authors:  Olga V Moroz; Maria Harkiolaki; Michael Y Galperin; Alexei A Vagin; Dolores González-Pacanowska; Keith S Wilson
Journal:  J Mol Biol       Date:  2004-10-01       Impact factor: 5.469

10.  House cleaning, a part of good housekeeping.

Authors:  Michael Y Galperin; Olga V Moroz; Keith S Wilson; Alexey G Murzin
Journal:  Mol Microbiol       Date:  2006-01       Impact factor: 3.501

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