This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Park, C. H.
Right arrow Articles by Byun, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Park, C. H.
Right arrow Articles by Byun, S. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2004, p. 6457-6464, Vol. 186, No. 19
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.19.6457-6464.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Hetero- and Autoprocessing of the Extracellular Metalloprotease (Mpr) in Bacillus subtilis

Chi Hye Park, Sang Jun Lee,{dagger} Sung Gu Lee, Weon Sup Lee, and Si Myung Byun*

Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, Korea

Received 23 March 2004/ Accepted 28 May 2004

Most proteases are synthesized as inactive precursors which are processed by proteolytic cleavage into a mature active form, allowing regulation of their proteolytic activity. The activation of the glutamic-acid-specific extracellular metalloprotease (Mpr) of Bacillus subtilis has been examined. Analysis of Mpr processing in defined protease-deficient mutants by activity assay and Western blotting revealed that the extracellular protease Bpr is required for Mpr processing. pro-Mpr remained a precursor form in bpr-deficient strains, and glutamic-acid-specific proteolytic activity conferred by Mpr was not activated in bpr-deficient strains. Further, purified pro-Mpr was processed to an active form by purified Bpr protease in vitro. We conclude that Mpr is activated by Bpr in vivo, and that heteroprocessing, rather than autoprocessing, is the major mechanism of Mpr processing in vivo. Exchange of glutamic acid for serine in the cleavage site of Mpr (S93E) allowed processing of Mpr into its mature form, regardless of the presence of other extracellular proteases, including Bpr. Thus, a single amino acid change is sufficient to convert the Mpr processing mechanism from heteroprocessing to autoprocessing.

* Corresponding author. Mailing address: Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Gusong-dong, Yusong-gu, Daejeon, Korea. Phone: 82-42-8692622. Fax: 82-42-8692610. E-mail: smbyun{at}kaist.ac.kr.

{dagger} Present address: Metabolic Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology, Daejeon, Korea.

Journal of Bacteriology, October 2004, p. 6457-6464, Vol. 186, No. 19
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.19.6457-6464.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gasanov, E.V., Demidyuk, I.V., Shubin, A.V., Kozlovskiy, V.I., Leonova, O.G., Kostrov, S.V. (2008). Hetero- and auto-activation of recombinant glutamyl endopeptidase from Bacillus intermedius. Protein Eng Des Sel 21: 653-658 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»