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Journal of Bacteriology, February 2005, p. 1519-1522, Vol. 187, No. 4
0021-9193/05/$08.00+0     doi:10.1128/JB.187.4.1519-1522.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mutational Alterations of the Key cis Proline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily

Hiroshi Kadokura, Lorenzo Nichols II,{dagger} and Jon Beckwith*

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts

Received 5 August 2004/ Accepted 2 November 2004

The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins. Conversion of the conserved cis proline 151 of DsbA to several hydrophilic residues results in accumulation of mixed disulfides between DsbA and its dedicated oxidant, DsbB. However, only a proline-to-threonine change causes accumulation of mixed disulfides of DsbA with its substrates.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-1920. Fax: (617) 738-7664. E-mail: jbeckwith{at}hms.harvard.edu.

{dagger} Present address: Department of Biological Sciences, University of Nevada Las Vegas, Las Vegas, NV 89154.

Journal of Bacteriology, February 2005, p. 1519-1522, Vol. 187, No. 4
0021-9193/05/$08.00+0     doi:10.1128/JB.187.4.1519-1522.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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