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PMID: 7751302 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The dnaA gene of Rhizobium meliloti lies within an unusual gene arrangement.

Journal of bacteriology ·Vol. 177 ·No. 10 ·1995-05-00 ·Pages 2892-900

Margolin W, Bramhill D, Long SR

Abstract

Rhizobium meliloti exists either as a free-living soil organism or as a differentiated endosymbiont bacteroid form within the nodules of its host plant, alfalfa (Medicago sativa), where it fixes atmospheric N2. Differentiation is accompanied by major changes in DNA replication and cell division. In addition, R. meliloti harbors three unique large circular chromosome-like elements whose replication coordination may be complex. As part of a study of DNA replication control in R. meliloti, we isolated a dnaA homolog. The deduced open reading frame predicts a protein of 57 kDa that is 36% identical to the DnaA protein of Escherichia coli, and the predicted protein was confirmed by immunoblot analysis. In a comparison with the other known DnaA proteins, this protein showed the highest similarity to that of Caulobacter crescentus and was divergent in some domains that are highly conserved in other unrelated species. The dnaA genes of a diverse group of bacteria are adjacent to a common set of genes. Surprisingly, analysis of the DNA sequence flanking dnaA revealed none of these genes, except for an rpsT homolog, also found upstream of dnaA in C. crescentus. Instead, upstream of rpsT lie homologs of fpg, encoding a DNA glycosylase, and fadB1, encoding an enoyl-coenzyme A hydratase with a strikingly high (53 to 55%) level of predicted amino acid identity to two mammalian mitochondrial homologs. Downstream of dnaA, there are two open reading frames that are probably expressed but are not highly similar to any genes in the databases. These results show that R. meliloti dnaA is located within a novel gene arrangement.

Related Genes
dnaA fadB1 rpsT
MeSH Terms
Amino Acid Sequence Bacteria/genetics Bacterial Proteins/genetics Base Sequence Biological Evolution Caulobacter/genetics Conserved Sequence DNA-Binding Proteins/genetics Enoyl-CoA Hydratase/genetics Genes, Bacterial/genetics Genomic Library Mitochondria/enzymology,genetics Molecular Sequence Data Open Reading Frames/genetics Restriction Mapping Ribosomal Proteins/genetics Sequence Analysis, DNA Sequence Homology, Amino Acid Sinorhizobium meliloti/genetics
Chemicals
Bacterial Proteins DNA-Binding Proteins DnaA protein, Bacteria Ribosomal Proteins ribosomal protein S20 Enoyl-CoA Hydratase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Margolin W
Department of Biological Sciences, Stanford University, California 94305-5020, USA.
Bramhill D
Long S R
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.177.10.2892-2900.1995
Published
1995-05-00
Pages
2892-900
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC176964
Subset
IM
Grants
NIGMS NIH HHS · 2R01-GM30962 · United States
Databases
GENBANK
L39265
SWISSPROT
UNKNOWN
External Links
PubMed source DOI: 10.1128/jb.177.10.2892-2900.1995 PMC Full Text View journal details
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