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Journal of Bacteriology, February 2005, p. 884-889, Vol. 187, No. 3
0021-9193/05/$08.00+0     doi:10.1128/JB.187.3.884-889.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Heat Shock Proteome Analysis of Wild-Type Corynebacterium glutamicum ATCC 13032 and a Spontaneous Mutant Lacking GroEL1, a Dispensable Chaperone

Institute of Biotechnology of León, INBIOTEC, Parque Científico de León,¹ Área de Microbiología, Fac. CC. Biológicas y Ambientales, Universidad de León,, León, Spain,³ Institut für Genomforschung, Universität Bielefeld, Bielefeld, Germany²

Received 20 September 2004/ Accepted 26 October 2004

Proteome analysis of Corynebacterium glutamicum ATCC 13032 showed that levels of several proteins increased drastically in response to heat shock. These proteins were identified as DnaK, GroEL1, GroEL2, ClpB, GrpE, and PoxB, and their heat response was in agreement with previous transcriptomic results. A major heat-induced protein was absent in the proteome of strain 13032B of C. glutamicum, used for genome sequencing in Germany, compared with the wild-type ATCC 13032 strain. The missing protein was identified as GroEL1 by matrix-assisted laser desorption ionization-time of flight peptide mass fingerprinting, and the mutation was found to be due to an insertion sequence, IsCg1, that was integrated at position 327 downstream of the translation start codon of the groEL1 gene, resulting in a truncated transcript of this gene, as shown by Northern analysis. The GroEL1 chaperone is, therefore, dispensable in C. glutamicum. On the other hand, GroEL2 appears to be essential for growth. Based on these results, the role of the duplicate groEL1 and groEL2 genes is analyzed.

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