Ribosomal RNA identity elements for ricin A-chain recognition and catalysis

Glück, Anton; Endo, Yaeta; Wool, Ira G.

doi:10.1016/0022-2836(92)90956-k

Cited by 118 publications

(86 citation statements)

References 35 publications

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“…Certain tetraloop sequences, such as the GAAA motif in SL1, occur in many RNAs and have been shown to increase stability of RNA molecules (Woese et al, 1990), participate in tertiary contacts (Jaeger et al, 1994;Murphy & Cech, 1994;Cate et al, 1996a), and serve as protein recognition sites (Gluck et al, 1992;Zwieb, 1992;De Guzman et al, 1998). Although the GNRA motif is conserved in all PVX strains, our data indicate that several changes in the GAAA tetraloop of SL1 are tolerated and that a GNRA tetraloop is not absolutely required for RNA accumulation.…”

Section: Discussionmentioning

confidence: 76%

Stem-loop structure in the 5′ region of potato virus X genome required for plus-strand RNA accumulation

Miller

Plante

Kim

et al. 1998

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 76%

Stem-loop structure in the 5′ region of potato virus X genome required for plus-strand RNA accumulation

Miller

Plante

Kim

et al. 1998

Journal of Molecular Biology

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“…1). Presence of a tetraloop structure could increase the stability of RNA duplexes or participate in RNA-RNA interactions or RNA-protein interactions (Cheong et al 1990;Gluck et al 1992;Jaeger et al 1994). Structure footprinting analysis of the yeast RNase P has indicated that the eP9 tetraloop is protected in the presence of protein subunits (Tranguch et al 1994).…”

Section: Discussionmentioning

confidence: 99%

Characterization of conserved sequence elements in eukaryotic RNase P RNA reveals roles in holoenzyme assembly and tRNA processing

Xiao

Day-Storms

Srisawat

et al. 2005

RNA

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RNase P is a ubiquitous endoribonuclease responsible for cleavage of the 5 0 leader of precursor tRNAs (pre-tRNAs). Although the protein composition of RNase P holoenzymes varies significantly among Bacteria, Archaea, and Eukarya, the holoenzymes have essential RNA subunits with several sequences and structural features that are common to all three kingdoms of life. Additional structural elements of the RNA subunits have been found that are conserved in eukaryotes, but not in bacteria, and might have functions specifically required by the more complex eukaryotic holoenzymes. In this study, we have mutated four eukaryotic-specific conserved regions in Saccharomyces cerevisiae nuclear RNase P RNA and characterized the effects of the mutations on cell growth, enzyme function, and biogenesis of RNase P. RNase P with mutations in each of the four regions tested is sufficiently functional to support life although growth of the resulting yeast strains was compromised to varying extents. Further analysis revealed that mutations in three different regions cause differential defects in holoenzyme assembly, localization, and pre-tRNA processing in vivo and in vitro. These data suggest that most, but not all, eukaryotic-specific conserved regions of RNase P RNA are important for the maturation and function of the holoenzyme.

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“…The fungal eP8 stem-loop structures have the NUGAG sequence (N = A, U, C, or G), whereas most of the eP9 hairpins contain GNRA (R = purine) tetraloops (15). Studies of hairpins from ribosomal RNA and other sources have suggested that a tetraloop structure could increase the thermodynamic stability of an RNA duplex, or act as a docking site for intramolecular or intermolecular RNA-RNA interactions (124)(125)(126)(127)(128)(129)(130). In E. coli RNase P RNA (M1 RNA), a mutation in the L9 loop results in a reduction in K m and k cat of the holoenzyme-catalyzed reaction with pre-4.5S RNA as substrate (131), but little effect on pre-tRNA processing in vitro.…”

Section: (18)mentioning

confidence: 99%

Eukaryotic Ribonuclease P: A Plurality of Ribonucleoprotein Enzymes

Xiao

Scott

Fierke³

et al. 2002

Annu. Rev. Biochem.

126

106

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Ribonuclease P (RNase P) is an essential endonuclease that acts early in the tRNA biogenesis pathway. This enzyme catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5′ end of tRNAs. RNase P activities have been identified in Bacteria, Archaea, and Eucarya, as well as organelles. Most forms of RNase P are ribonucleoproteins, i.e. they consist of an essential RNA subunit and protein subunits, although the composition of the enzyme in mitochondria and chloroplasts is still under debate. The recent purification of the eukaryotic nuclear RNase P has demonstrated a significantly larger protein content compared to the bacterial enzyme. Moreover, emerging evidence suggests that the eukaryotic RNase P has evolved into at least two related nuclear enzymes with distinct functions, RNase P and RNase MRP. Here we review current information on RNase P, with emphasis on the composition, structure, and functions of the eukaryotic nuclear holoenzyme, and its relationship with RNase MRP.

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Ribosomal RNA identity elements for ricin A-chain recognition and catalysis

Cited by 118 publications

References 35 publications

Stem-loop structure in the 5′ region of potato virus X genome required for plus-strand RNA accumulation

Stem-loop structure in the 5′ region of potato virus X genome required for plus-strand RNA accumulation

Characterization of conserved sequence elements in eukaryotic RNase P RNA reveals roles in holoenzyme assembly and tRNA processing

Eukaryotic Ribonuclease P: A Plurality of Ribonucleoprotein Enzymes

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