Skip Navigation

This Article
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 Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Matsuzaki, M.
Right arrow Articles by Satoh, T.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Matsuzaki, M.
Right arrow Articles by Satoh, T.
Agricola
Right arrow Articles by Matsuzaki, M.
Right arrow Articles by Satoh, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1996, Vol. 37, No. 3 333-339
© 1996

Stabilization by GroEL, a Molecular Chaperone, and a Periplasmic Fraction, as Well as Refolding in the Presence of Dithiothreitol, of Acid-Unfolded Dimethyl Sulfoxide Reductase, a Periplasmic Protein of Rhodobacter sphaeroides f. sp. denitrificans

Masahiro Matsuzaki, Yoko Yamaguchi, Hideo Masui and Toshio Satoh

Department of Biological Science, Faculty of Science, Hiroshima University Higashi-Hiroshima, 739 Japan

The mechanisms of folding of a periplasmic protein was studied in vitro using dimethyl sulfoxide reductase (DMSOR), a periplasmic enzyme of Rhodobacter sphaeroides f. sp. denitrificans. When DMSOR was denatured by acidification to pH 2 at 30°C, the molybdenum cofactor was immediately released and unfolded forms of DMSOR appeared within 2 min. When the acid-unfolded DMSOR has been incubated in refolding buffer (pH 8.0) at 20°C for 2 h, it became almost undetectable after electrophoresis on a non-denaturing gel. This result suggests that the acid-unfolded DMSOR might have aggregated after incubation. The aggregation was suppressed by incubation in the presence of commercial GroEL, a molecular chaperone. When reduced dithiothreitol (DTT) was added to the acid-unfolded forms in the presence of GroEL, some of the DMSOR was converted to the native form, which had the same mobility on a non-denaturing gel as the active emzyme. Non-reducing SDS-polyacrylamide gel electrophoresis of the acid-unfolded forms of DMSOR indicated that the unfolded forms were a mixture of heterogeneously folded or misfolded forms and that their forms were converted by DTT to the fully reduced form. The periplasmic fraction of the phototroph was also able to suppress the aggregation of the acid-unfolded DMSOR, and a protein(s) with a molecular mass of about 40 kDa in the periplasm was revealed to have stabilizing activity. It appears that there exists a mechanism whereby the unfolded DMSOR that is secreted into the periplasm is maintained in a non-aggregated and reduced form during folding to the native form.

(Received November 4, 1995; Accepted February 8, 1996)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
M. Matsuzaki, M. Abe, S. Hara, Y. Iwasaki, I. Yamamoto, and T. Satoh
An Abundant Periplasmic Protein of the Denitrifying Phototroph Rhodobacter sphaeroides f. sp. denitrificans is PstS, a Component of an ABC Phosphate Transport System
Plant Cell Physiol., February 15, 2003; 44(2): 212 - 216.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
M. Matsuzaki, Y. Kiso, I. Yamamoto, and T. Satoh
Isolation of a Periplasmic Molecular Chaperone-Like Protein of Rhodobacter sphaeroides f. sp. denitrificans That Is Homologous to the Dipeptide Transport Protein DppA of Escherichia coli
J. Bacteriol., May 15, 1998; 180(10): 2718 - 2722.
[Abstract] [Full Text]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.