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Limited Stress Response in Streptococcus pneumoniae
Author(s) -
Choi Inhwa,
Shim Jaiheon,
Kim Seungwhan,
Kim Sunam,
Pyo Suhkneung,
Rhee Dongkwon
Publication year - 1999
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1999.tb02474.x
Subject(s) - groel , heat shock protein , streptococcus pneumoniae , biology , bacillus subtilis , microbiology and biotechnology , escherichia coli , heat shock , hsp60 , alcohol dehydrogenase , shock (circulatory) , thermal shock , chaperonin , bacteria , biochemistry , hsp70 , ethanol , gene , genetics , antibiotics , medicine , materials science , composite material
In Streptococcus pneumoniae , heat shock induces the synthesis of 65‐, 73‐, and 84‐kDa proteins, and ethanol shock induces a 104‐kDa protein. In this study, the 65‐, 84‐, and 104‐kDa proteins were identified as members of the GroEL, ClpL and alcohol dehydrogenase families, respectively, and the general properties of the stress response of S. pneumoniae to several other stresses were characterized. However, several stresses which are known to induce stress responses in Escherichia coli and Bacillus subtilis failed to induce any high molecular weight heat‐shock proteins (HSPs) such as GroEL and DnaK homologues. A minor temperature shift from 30 to 37 C triggered induction of the homologues of DnaK and GroEL of E. coli . These features may provide a foundation for evaluating the role of heat‐shock proteins relative to the physiology and pathogenesis of pneumococcus.