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Split dnaE genes encoding multiple novel inteins in Trichodesmium erythraeum.

Xiang-Qin Liu1, Jing Yang

  • 1Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada. pxqliu@dal.ca

The Journal of Biological Chemistry
|May 27, 2003
PubMed
Summary

Three novel inteins were discovered in Trichodesmium erythraeum

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cyanobacteria Research

Background:

  • Inteins are protein segments that can excise themselves from a precursor protein.
  • The dnaE gene encodes the catalytic subunit of DNA polymerase III, crucial for DNA replication.
  • Split inteins are found on separate polypeptides but can join together to catalyze splicing.

Purpose of the Study:

  • To identify and characterize inteins within the dnaE gene of Trichodesmium erythraeum.
  • To investigate the structure and potential function of these inteins, particularly DnaE-1, DnaE-2, and DnaE-3.
  • To understand the mechanism of DnaE protein synthesis involving these inteins.

Main Methods:

  • Bioinformatic analysis of the dnaE gene sequence.
  • In silico prediction of intein structures and domains.
  • Heterologous expression and functional testing of inteins in Escherichia coli.

Main Results:

  • Three inteins (DnaE-1, DnaE-2, DnaE-3) were identified in a clustered region of the Trichodesmium erythraeum DnaE protein.
  • DnaE-1 is unusually large (1258 aa) due to tandem repeats, which inhibited its splicing activity.
  • DnaE-2 is of typical size with predicted splicing and endonuclease domains, while DnaE-3 is a split intein.
  • A complex synthesis pathway involving cis- and trans-splicing reactions is predicted for mature DnaE protein.

Conclusions:

  • The unique intein structures in Trichodesmium erythraeum's DnaE suggest novel mechanisms for regulating DNA replication.
  • The tandem repeats in DnaE-1 may serve as a regulatory element controlling DnaE synthesis.
  • Further research is needed to elucidate the precise roles and regulation of these inteins in vivo.

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