ArticleApplied and environmental microbiology2005
Quantitative analysis of group II intron expression and splicing in Lactococcus lactis.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Group II Introns Generate Functional Chimeric Relaxase Enzymes with Modified Specificities through Exon Shuffling at Both the RNA and DNA Level.Molecular biology and evolution · 2021Article
- Article
- Mobile self-splicing introns and inteins as environmental sensors.Current opinion in microbiology · 2017Review
- Interaction between conjugative and retrotransposable elements in horizontal gene transfer.PLoS genetics · 2014Article
- Article
- Splicing of the Sinorhizobium meliloti RmInt1 group II intron provides evidence of retroelement behavior.Nucleic acids research · 2011Article
- Survey of group I and group II introns in 29 sequenced genomes of the Bacillus cereus group: insights into their spread and evolution.Nucleic acids research · 2008Article
- Dispersion of the RmInt1 group II intron in the Sinorhizobium meliloti genome upon acquisition by conjugative transfer.Nucleic acids research · 2007Article
- Trans-splicing of the Ll.LtrB group II intron in Lactococcus lactis.Nucleic acids research · 2007Article
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4 authors.
Funding
Abstract
The group II intron Ll.ltrB is found within the ltrB relaxase gene of the conjugative element pRS01 in Lactococcus lactis. Precise splicing of the intron is essential for pRS01 transfer. The transcription regulation and in vivo splicing activity of Ll.ltrB have not been investigated thoroughly in L. lactis in the natural pRS01 context. We developed absolute quantitative real-time reverse transcription-PCR assays to quantify RNA levels of the 5' exon (ltrBE1) and the spliced relaxase (ltrB) and intron-encoded protein (ltrA) genes, as well as Ll.ltrB splicing activity under different physiological conditions. The mRNA levels for the ATP-binding protein OppD were assayed for comparison to the ltrB transcripts. The oppD mRNA ranged from 10- to 10,000-fold higher than ltrB region genes. ltrBE1 expression was growth-phase dependent. The mRNA level of ltrA was almost constant during all growth phases and in all media tested. Ll.ltrB in vivo splicing activity ranged from (6.5 +/- 2.1)% to (22.1 +/- 8.0)%. Acid challenge significantly decreased both ltrB region mRNA levels and intron splicing activity. The presence of recipient cells, different mating environments, and temperature stress had no significant effects on expression and splicing. Western blotting showed that the level of LtrB protein expressed from an intronless ltrB gene was much higher (about 20-fold) than the level of protein expressed from an intron-containing construct. Interestingly, LtrB protein showed a tendency to function in cis on its oriT target. The low level of ltrB transcript and relatively inefficient splicing of the intron may limit Ll.ltrB mobility and dissemination in nature.
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