Comparative Proteomic Analysis of Lactobacillus plantarum WCFS1 and ΔctsR Mutant Strains Under Physiological and Heat Stress Conditions

International Journal of Molecular Sciences

Pasquale Russo²  Mar໚ de la Luz Mohedano¹  Vittorio Capozzi²  Pilar Fernández de Palencia¹  Paloma López¹  Giuseppe Spano² 

[1] Biology Research Center, Department of Molecular Microbiology and Infection Biology, calle Ramiro de Maetzu 9, Madrid 28040, Spain; E-Mails:;Department of Agriculture, Food and Environment Sciences, Via Napoli 25, Foggia 71122, Italy; E-Mails:

关键词: ClpE;    CtsR;    heat;    Lactobacillus plantarum;    stress;   

DOI  :  10.3390/ijms130910680

来源: mdpi

【 摘 要 】

Among Gram-positive bacteria, CtsR (Class Three Stress gene Repressor) mainly regulates the expression of genes encoding the Clp ATPases and the ClpP protease. To gain a better understanding of the biological significance of the CtsR regulon in response to heat-shock conditions, we performed a global proteomic analysis of Lactobacillus plantarum WCFS1 and ΔctsR mutant strains under optimal or heat stress temperatures. Total protein extracts from bacterial cells were analyzed by two-dimensional gel fractionation. By comparing maps from different culture conditions and different L. plantarum strains, image analysis revealed 23 spots with altered levels of expression. The proteomic analysis of L. plantarum WCFS1 and ctsR mutant strains confirms at the translational level the CtsR-mediated regulation of some members of the Clp family, as well as the heat induction of typical stress response genes. Heat activation of the putative CtsR regulon genes at transcriptional and translational levels, in the ΔctsR mutant, suggests additional regulative mechanisms, as is the case of hsp1. Furthermore, isoforms of ClpE with different molecular mass were found, which might contribute to CtsR quality control. Our results could add new outlooks in order to determine the complex biological role of CtsR-mediated stress response in lactic acid bacteria.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.