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PMID: 11880608 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A mitochondrial-like aconitase in the bacterium Bacteroides fragilis: implications for the evolution of the mitochondrial Krebs cycle.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 99 ·No. 7 ·2002-04-02 ·Pages 4662-7

Baughn AD, Malamy MH

Abstract

Aconitase and isocitrate dehydrogenase (IDH) enzyme activities were detected in anaerobically prepared cell extracts of the obligate anaerobe Bacteroides fragilis. The aconitase gene was located upstream of the genes encoding the other two components of the oxidative branch of the Krebs cycle, IDH and citrate synthase. Mutational analysis indicates that these genes are cotranscribed. A nonpolar in-frame deletion of the acnA gene that encodes the aconitase prevented growth in glucose minimal medium unless heme or succinate was added to the medium. These results imply that B. fragilis has two pathways for alpha-ketoglutarate biosynthesis-one from isocitrate and the other from succinate. Homology searches indicated that the B. fragilis aconitase is most closely related to aconitases of two other Cytophaga-Flavobacterium-Bacteroides (CFB) group bacteria, Cytophaga hutchinsonii and Fibrobacter succinogenes. Phylogenetic analysis indicates that the CFB group aconitases are most closely related to mitochondrial aconitases. In addition, the IDH of C. hutchinsonii was found to be most closely related to the mitochondrial/cytosolic IDH-2 group of eukaryotic organisms. These data suggest a common origin for these Krebs cycle enzymes in mitochondria and CFB group bacteria.

MeSH Terms
Aconitate Hydratase/chemistry,genetics,physiology Amino Acid Sequence Bacteroides fragilis/enzymology,genetics Biological Evolution Citric Acid Cycle Genes, Bacterial/physiology Isocitrate Dehydrogenase/metabolism Mitochondria/metabolism Molecular Sequence Data
Chemicals
Isocitrate Dehydrogenase Aconitate Hydratase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Baughn Anthony D
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Malamy Michael H
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.052710199
Published
2002-04-02
Epub
2002-00-05
Pages
4662-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC123704
Subset
IM
Grants
NIAID NIH HHS · R01 AI019497 · United States
NIAID NIH HHS · R21 AI019497 · United States
NIAID NIH HHS · AI-19497 · United States
Databases
GENBANK
AF434843
Corrections
CommentIn
PMID: 11929988
External Links
PubMed source DOI: 10.1073/pnas.052710199 PMC Full Text View journal details
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