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Title: MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria

Authors:
 [1];  [2];  [3];  [1];  [1];  [4];  [5];  [6];  [7]
  1. Univ. of California, Berkeley, CA (United States). Dept. of Plant and Microbial Biology
  2. Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cellular Biology; Univ. of California, Berkeley, CA (United States). California Institute for Quantitative Biosciences
  3. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Physical Biosciences Division
  4. Univ. of California, Berkeley, CA (United States). Dept. of Chemistry
  5. Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cellular Biology; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Physical Biosciences Division; Univ. of California, Berkeley, CA (United States). Dept. of Chemistry
  6. Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cellular Biology; Univ. of California, Berkeley, CA (United States). California Institute for Quantitative Biosciences; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Life Sciences Division
  7. Univ. of California, Berkeley, CA (United States). Dept. of Plant and Microbial Biology; Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cellular Biology; Univ. of California, Berkeley, CA (United States). California Institute for Quantitative Biosciences
Publication Date:
Research Org.:
University of California, Berkeley, CA (United States); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1253997
Alternate Identifier(s):
OSTI ID: 1379123; OSTI ID: 1379160
Grant/Contract Number:  
AC02-05CH11231; MR‐15‐328599; R01GM084122; N000141310421
Resource Type:
Accepted Manuscript
Journal Name:
PLoS Biology (Online)
Additional Journal Information:
Journal Name: PLoS Biology (Online); Journal Volume: 14; Journal Issue: 3; Journal ID: ISSN 1545-7885
Publisher:
Public Library of Science
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Hershey, David M., Ren, Xuefeng, Melnyk, Ryan A., Browne, Patrick J., Ozyamak, Ertan, Jones, Stephanie R., Chang, Michelle C. Y., Hurley, James H., and Komeili, Arash. MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria. United States: N. p., 2016. Web. doi:10.1371/journal.pbio.1002402.
Hershey, David M., Ren, Xuefeng, Melnyk, Ryan A., Browne, Patrick J., Ozyamak, Ertan, Jones, Stephanie R., Chang, Michelle C. Y., Hurley, James H., & Komeili, Arash. MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria. United States. https://doi.org/10.1371/journal.pbio.1002402
Hershey, David M., Ren, Xuefeng, Melnyk, Ryan A., Browne, Patrick J., Ozyamak, Ertan, Jones, Stephanie R., Chang, Michelle C. Y., Hurley, James H., and Komeili, Arash. Wed . "MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria". United States. https://doi.org/10.1371/journal.pbio.1002402. https://www.osti.gov/servlets/purl/1253997.
@article{osti_1253997,
title = {MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria},
author = {Hershey, David M. and Ren, Xuefeng and Melnyk, Ryan A. and Browne, Patrick J. and Ozyamak, Ertan and Jones, Stephanie R. and Chang, Michelle C. Y. and Hurley, James H. and Komeili, Arash},
abstractNote = {},
doi = {10.1371/journal.pbio.1002402},
journal = {PLoS Biology (Online)},
number = 3,
volume = 14,
place = {United States},
year = {Wed Mar 16 00:00:00 EDT 2016},
month = {Wed Mar 16 00:00:00 EDT 2016}
}

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Free Publicly Available Full Text
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Cited by: 30 works
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