Group II Introns and Their Protein Collaborators
Group II introns are an abundant class of autocatalytic introns that excise themselves from precursor mRNAs. Although group II introns are catalytic RNAs, they require the assistance of proteins for efficient splicing in vivo. Proteins that facilitate splicing of organellar group II introns fall into two main categories: intron-encoded maturases and host-encoded proteins. This chapter will focus on the host proteins that group II introns recruited to ensure their function. It will discuss the great diversity of these proteins, define common features, and describe different strategies employed to achieve specificity. Special emphasis will be placed on DEAD-box ATPases, currently the best studied example of host-encoded proteins with a role in group II intron splicing. Since the exact mechanisms by which splicing is facilitated is not known for any of the host proteins, general mechanistic strategies for protein-mediated RNA folding are described and assessed for their potential role in group II intron splicing.
KeywordsIntron Splice Pentatricopeptide Repeat Pentatricopeptide Repeat Protein Kinetic Trap Misfolded Structure
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- Belfort M, Derbyshire V, Parker MM, Cousineau B, Lambowitz AM (2001) Mobile introns: pathways and proteins. In: NL Craig, R Gragie, M Gellert, AM Lambowitz (eds.) Mobile DNA II. ASM Press, Washington, DC, pp. 761–782Google Scholar
- Bonen L (1993) Trans-splicing of pre-mRNA in plants, animals, and protists. FASEB J 7:40–46Google Scholar
- Halls C, Mohr S, Del Campo M, Yang Q, Jankowsky E, Lambowitz AM (2007) Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chap-erone activity. J Mol Biol 365:835–855CrossRefGoogle Scholar
- Herschlag D (1995) RNA chaperones and the RNA folding problem. J Biol Chem 270:20871–20874Google Scholar
- Lambowitz AM, Caprara MG, Zimmerly S, Perlman PS (1999) Group I and group II ribozymes as RNPs: clues to the past and guides to the future. In: RF Gesteland, TR Cech, JF Atkins (eds.) The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 451–485Google Scholar
- Lurin C, Andres C, Aubourg S, Bellaoui M, Bitton F, Bruyere C, Caboche M, Debast C, Gualberto J, Hoffmann B, Lecharny A, Le Ret M, Martin-Magniette ML, Mireau H, Peeters N, Renou JP, Szurek B, Taconnat L, Small I (2004) Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis. Plant Cell 16: 2089–2103CrossRefGoogle Scholar
- Pyle AM, Lambowitz AM (2006) Group II introns: ribozymes that splice RNA and invade DNA. In: RF Gesteland, TR Cech, JF Atkins (eds.) The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 469–506Google Scholar
- Tavares-Carreon F, Camacho-Villasana Y, Zamudio-Ochoa A, Shingu-Vazquez M, Torres-Larios A, Perez-Martinez X (2008) The pentatricopeptide repeats present in Pet309 are necessary for translation but not for stability of the mitochondrial COX1 mRNA in yeast. J Biol Chem 283:1472–1479CrossRefGoogle Scholar
- Tzagoloff A, Akai A, Needleman RB (1975) Assembly of the mitochondrial membrane system. Characterization of nuclear mutants of Saccharomyces cerevisiae with defects in mitochon-drial ATPase and respiratory enzymes. J Biol Chem 250:8228–8235Google Scholar
- Wiesenberger G, Waldherr M, Schweyen RJ (1992) The nuclear gene MRS2 is essential for the excision of group II introns from yeast mitochondrial transcripts in vivo. J Biol Chem 267:6963–6969Google Scholar