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J Bacteriol, May 1998, p. 2718-2722, Vol. 180, No. 10
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

Masahiro Matsuzaki, Yuso Kiso, Isamu Yamamoto, and Toshio Satoh*

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

Received 2 December 1997/Accepted 11 March 1998

A periplasmic protein has been found to prevent aggregation of the acid-unfolded dimethyl sulfoxide reductase (DMSOR), the periplasmic terminal reductase of dimethyl sulfoxide respiration in the phototroph Rhodobacter sphaeroides f. sp. denitrificans, in a manner similar to that of the Escherichia coli chaperonin GroEL (Matsuzaki et al., Plant Cell Physiol. 37:333-339, 1996). The protein was isolated from the periplasm of the phototroph. It had a molecular mass of 58 kDa and had no subunits. The sequence of 14 amino-terminal residues of the protein was completely identical to that of the periplasmic dipeptide transport protein (DppA) of E. coli. The 58-kDa protein prevented aggregation to a degree comparable to that of GroEL on the basis of monomer protein. The 58-kDa protein also decreased aggregation of guanidine hydrochloride-denatured rhodanese, a mitochondrial matrix protein, during its refolding upon dilution. The 58-kDa protein is a kind of molecular chaperone and could be involved in maintaining unfolded DMSOR, after secretion of the latter into the periplasm, in a competent form for its correct folding.

* Corresponding author. Mailing address: Department of Biological Science, Faculty of Science, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima 739-8526, Japan. Phone: 81-824-24-7453. Fax: 81-824-24-0734. E-mail: satoht{at}ipc.hiroshima-u.ac.jp.

J Bacteriol, May 1998, p. 2718-2722, Vol. 180, No. 10
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Matsuzaki, M., Abe, M., Hara, S., Iwasaki, Y., Yamamoto, I., Satoh, T. (2003). 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 44: 212-216 [Abstract] [Full Text]  
  • Cho, W. J., Yoon, W. J., Moon, C. H., Cha, S. J., Song, H., Cho, H. R., Jang, S. J., Chung, D. K., Jeong, C. S., Park, J. W. (2002). Molecular Cloning of a Novel Chaperone-like Protein Induced by Rhabdovirus Infection with Sequence Similarity to the Bacterial Extracellular Solute-binding Protein Family 5. J. Biol. Chem. 277: 41489-41496 [Abstract] [Full Text]  


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