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Journal of Bacteriology, November 2001, p. 6282-6287, Vol. 183, No. 21
Faculty of Pharmaceutical Sciences,
Kobe-Gakuin University, Nishi-ku, Kobe 651-2180, Japan,1 and Department of Biochemistry,
Robert Wood Johnson Medical School, Piscataway, New Jersey
088542
Received 14 June 2001/Accepted 7 August 2001
Optimal conditions for two-dimensional gel electrophoresis of total
cellular proteins from Myxococcus xanthus were established. Using these conditions, we analyzed protein patterns of heat-shocked M. xanthus cells. Eighteen major spots and 15 minor spots
were found to be induced by heat shock. From N-terminal sequences of 15 major spots, DnaK, GroEL, GroES, alkyl hydroperoxide reductase, aldehyde dehydrogenase, succinyl coenzyme A (CoA) synthetase, 30S
ribosomal protein S6, and ATP synthase
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.21.6282-6287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Heat-Shock-Induced Proteins from
Myxococcus xanthus
subunit were identified. Three of the 18 major spots had an identical N-terminal sequence, indicating that they may be different forms of the same protein. Although a DnaK homologue, SglK, has been identified in M. xanthus (R. M. Weimer, C. Creghton, A. Stassinopoulos, P. Youderian, and P. L. Hartzell, J. Bacteriol. 180:5357-5368, 1998;
Z. Yang, Y. Geng, and W. Shi, J. Bacteriol. 180:218-224, 1998), SglK
was not induced by heat shock. In addition, there were seven
substitutions within the N-terminal 30-residue sequence of the newly
identified DnaK. This is the first report to demonstrate that
succinyl CoA synthetase, 30S ribosomal protein S6, and ATP synthase
subunit are heat shock inducible.
*
Corresponding author. Mailing address: Department of
Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Ln.,
Piscataway, NJ 08854. Phone: (732) 235-4161. Fax: (732) 235-4559. E-mail: sinouye{at}waksman.rutgers.edu.
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