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Bacillus subtilis aconitase is an RNA-binding protein.
Proc Natl Acad Sci U S A. 1999 Aug 31; 96(18):10412-7.PN

Abstract

The aconitase protein of Bacillus subtilis was able to bind specifically to sequences resembling the iron response elements (IREs) found in eukaryotic mRNAs. The sequences bound include the rabbit ferritin IRE and IRE-like sequences in the B. subtilis operons that encode the major cytochrome oxidase and an iron uptake system. IRE binding activity was affected by the availability of iron both in vivo and in vitro. In eukaryotic cells, aconitase-like proteins regulate translation and stability of iron metabolism mRNAs in response to iron availability. A mutant strain of B. subtilis that produces an enzymatically inactive aconitase that was still able to bind RNA sporulated 40x more efficiently than did an aconitase null mutant, suggesting that a nonenzymatic activity of aconitase is important for sporulation. The results support the idea that bacterial aconitases, like their eukaryotic homologs, are bifunctional proteins, showing aconitase activity in the presence of iron and RNA binding activity when cells are iron-deprived.

Authors+Show Affiliations

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.No affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

10468622

Citation

Alén, C, and A L. Sonenshein. "Bacillus Subtilis Aconitase Is an RNA-binding Protein." Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 18, 1999, pp. 10412-7.
Alén C, Sonenshein AL. Bacillus subtilis aconitase is an RNA-binding protein. Proc Natl Acad Sci U S A. 1999;96(18):10412-7.
Alén, C., & Sonenshein, A. L. (1999). Bacillus subtilis aconitase is an RNA-binding protein. Proceedings of the National Academy of Sciences of the United States of America, 96(18), 10412-7.
Alén C, Sonenshein AL. Bacillus Subtilis Aconitase Is an RNA-binding Protein. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10412-7. PubMed PMID: 10468622.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Bacillus subtilis aconitase is an RNA-binding protein. AU - Alén,C, AU - Sonenshein,A L, PY - 1999/9/1/pubmed PY - 1999/9/1/medline PY - 1999/9/1/entrez SP - 10412 EP - 7 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 96 IS - 18 N2 - The aconitase protein of Bacillus subtilis was able to bind specifically to sequences resembling the iron response elements (IREs) found in eukaryotic mRNAs. The sequences bound include the rabbit ferritin IRE and IRE-like sequences in the B. subtilis operons that encode the major cytochrome oxidase and an iron uptake system. IRE binding activity was affected by the availability of iron both in vivo and in vitro. In eukaryotic cells, aconitase-like proteins regulate translation and stability of iron metabolism mRNAs in response to iron availability. A mutant strain of B. subtilis that produces an enzymatically inactive aconitase that was still able to bind RNA sporulated 40x more efficiently than did an aconitase null mutant, suggesting that a nonenzymatic activity of aconitase is important for sporulation. The results support the idea that bacterial aconitases, like their eukaryotic homologs, are bifunctional proteins, showing aconitase activity in the presence of iron and RNA binding activity when cells are iron-deprived. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/10468622/Bacillus_subtilis_aconitase_is_an_RNA_binding_protein_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=10468622 DB - PRIME DP - Unbound Medicine ER -