Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2009 Oct;191(20):6193-202.
doi: 10.1128/JB.00675-09. Epub 2009 Aug 7.

Group I introns and inteins: disparate origins but convergent parasitic strategies

Affiliations
Review

Group I introns and inteins: disparate origins but convergent parasitic strategies

Rahul Raghavan et al. J Bacteriol. 2009 Oct.
No abstract available

PubMed Disclaimer

Figures

FIG. 1.
FIG. 1.
(A) Predicted secondary structure of a group I intron (Cbu.L1951) (93). Paired, conserved helices common to group I introns are designated P1 to P10. The 5′- and 3′-terminal intron bases are encircled. The intron sequence is in uppercase; 5′ and 3′ exons are in lowercase and colored red and blue, respectively. P1 and P10 together form the IGS. The site of HE insertion in P8 is indicated in green. (B) Mechanism of group I intron splicing (110). 5′ and 3′ exons are in red and blue, respectively. ΩG, terminal intron guanine. G*, exogenous guanosine. (Step 1) Nucleophilic attack on the 5′ splice site by the 3′-OH of G* in GBS. (Step 2) Nucleophilic attack on the 3′ splice site by the free 3′-OH of the 5′ exon. (Step 3) Free intron and spliced exons.
FIG. 2.
FIG. 2.
(A) Intein modular structure (87, 90). An intein with flanking exteins is shown. The N- and C-terminal splicing domains and the optional HE domain with their conserved motifs are shown. Conserved amino acids Cys or Ser at the 5′ end of the intein, Asn at the 3′ end of the intein, and Cys, Ser, or Thr at the first position on the 3′ extein are also indicated. (B) Intein splicing chemistry (39, 87). N and C exteins are in red and blue, respectively.
FIG. 3.
FIG. 3.
(A) Intein or group I intron homing through HE-mediated DNA double-strand-break repair and recombination. (B) Cycle model of HE gain, degeneration, and loss within host populations (37, 38, 39).
FIG. 4.
FIG. 4.
Convergence of evolutionary paths of group I introns, inteins, and HEs.

Similar articles

Cited by

References

    1. Aagaard, C., J. Z. Dalgaard, and R. A. Garrett. 1995. Intercellular mobility and homing of an archaeal rDNA intron confers a selective advantage over intron− cells of Sulfolobus acidocaldarius. Proc. Natl. Acad. Sci. USA 92:12285-12289. - PMC - PubMed
    1. Amitai, G., O. Belenkiy, B. Dassa, A. Shainskaya, and S. Pietrokovski. 2003. Distribution and function of new bacterial intein-like protein domains. Mol. Microbiol. 47:61-73. - PubMed
    1. Amitai, G., B. Dassa, and S. Pietrokovski. 2004. Protein splicing of inteins with atypical glutamine and aspartate C-terminal residues. J. Biol. Chem. 279:3121-3131. - PubMed
    1. Avise, J. C. 2001. Evolving genomic metaphors: a new look at the language of DNA. Science 294:86-87. - PubMed
    1. Ayre, B. G., U. Köhler, H. M. Goodman, and J. Haseloff. 1999. Design of highly specific cytotoxins by using trans-splicing ribozymes. Proc. Natl. Acad. Sci. USA 96:3507-3512. - PMC - PubMed

Publication types

LinkOut - more resources