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Related Experiment Videos

A bacterial group II intron-encoded reverse transcriptase localizes to cellular poles.

Junhua Zhao1, Alan M Lambowitz

  • 1Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, and Section of Molecular Genetics and Microbiology, University of Texas, Austin, TX 78712, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 28, 2005
PubMed
Summary

The LtrA protein from Lactococcus lactis localizes to cellular poles in bacteria, independent of intron RNA. This localization may influence Ll.LtrB intron insertion and link mobility to host cell machinery.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • The Ll.LtrB group II intron in Lactococcus lactis utilizes a reverse transcriptase (LtrA protein) for RNA splicing and mobility.
  • Understanding the spatial organization of such mobile genetic elements is crucial for deciphering their life cycle and interactions with host cells.

Purpose of the Study:

  • To investigate the cellular localization of the LtrA protein in bacterial hosts.
  • To determine factors influencing LtrA localization and its potential functional implications.

Main Methods:

  • Utilized LtrA-green fluorescent protein (GFP) fusions.
  • Employed immunofluorescence microscopy in Escherichia coli and Lactococcus lactis.
  • Assessed localization patterns under varying conditions (intron RNA coexpression, growth rates, expression levels).

Related Experiment Videos

  • Examined LtrA subsegment localization and interference with IcsA protein localization.

    • Main Results:

    • LtrA protein consistently localized to cellular poles in both E. coli and L. lactis.
    • Polar localization was observed irrespective of Ll.LtrB intron RNA presence, growth conditions, or replication origin function.
    • Specific LtrA subsegments also exhibited polar localization, suggesting redundant signals or inherent protein properties.
    • LtrA interfered with the polar localization of Shigella IcsA protein in E. coli, indicating competition for localization determinants.

    Conclusions:

    • LtrA protein possesses intrinsic properties driving polar localization in bacterial cells.
    • This polar localization may direct Ll.LtrB intron insertion to specific chromosomal regions (origin/terminus).
    • LtrA's localization could link group II intron mobility to host DNA replication and cell division processes.