Open AccessA rubrerythrin‐like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21
Author(s) -
May Antje,
Hillmann Falk,
Riebe Oliver,
Fischer RalfJörg,
Bahl Hubert
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09763.x
Subject(s) - clostridium acetobutylicum , heat shock protein , rubredoxin , open reading frame , gene , chemistry , anaerobic bacteria , biochemistry , biology , bacteria , genetics , peptide sequence , butanol , ethanol
Comparison of the N‐terminus of the heat shock protein Hsp21 of Clostridium acetobutylicum with proteins predicted to be encoded by the genome of this bacterium revealed that this stress protein is encoded by two almost identical open reading frames CAC3597 and CAC3598. These genes encode a rubrerythrin‐like protein with the rubredoxin‐like FeS 4 domain at the N‐terminus and the ferritin‐like diiron domain (rubrerythrin domain) at the C‐terminus. Thus, the order of the two putative functional domains is reversed compared to “normal” rubrerythrins. This protein is proposed to be involved in the oxidative stress response of strict anaerobic bacteria. Northern blot analysis indicated that hsp21 is induced by heat and oxidative stress (air, H 2 O 2 ). Hsp21 of C. acetobutylicum can be considered as a “reverse” rubrerythrin and a role of this stress protein, which is conserved among clostridia and other strict anaerobic bacteria, in the heat and oxidative stress response is proposed.