Mechanistic Studies of the Spore Photoproduct Lyase via a Single Cysteine Mutation-Reference-Cited by-同舟云学术

Mechanistic Studies of the Spore Photoproduct Lyase via a Single Cysteine Mutation

Published:2012-08-31 Issue:36 Volume:51 Page:7173-7188
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Yang Linlin¹,Lin Gengjie¹,Nelson Renae S.¹,Jian Yajun¹,Telser Joshua²,Li Lei¹³

Affiliation:

1. Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 North Blackford Street, Indianapolis, Indiana 46202, United States

2. Department of Biological, Chemical, and Physical Sciences, Roosevelt University, Chicago, Illinois 60605, United States

3. Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, Indiana 46202, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3010945

Reference98 articles.

1. Spore Photoproduct: A Key to Bacterial Eternal Life

2. Binding of DNA in vitro by a small, acid-soluble spore protein from Bacillus subtilis and the effect of this binding on DNA topology

3. Binding of small acid-soluble spore proteins from Bacillus subtilis changes the conformation of DNA from B to A.

4. Ultraviolet irradiation of DNA complexed with alpha/beta-type small, acid-soluble proteins from spores of Bacillus or Clostridium species makes spore photoproduct but not thymine dimers.

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