If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Nucleosides and Nucleotides Biosynthesis → Nucleic Acid Processing|
Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655
Expected Taxonomic Range:
tRNAs are the molecular adapters that allow the synthesis of proteins based on mRNAs transcribed from protein-coding genes. The active form of tRNA is generated by a combination of nuclease-based processing, the modification of select nucleosides, and finally charging via the tRNA charging.
tRNA processing is a multi-step pathway carried out by a mix of endonucleases and exonucleases. Processing begins with the endonucleolytic cleavage of individual tRNA precursors from RNAs containing multiple tRNAs. This initial cleavage can generate precursor molecules with a long 5' trailing end or with a short 5' extension. Precursors with a long trailer require additional exonucleolytic processing before the other nucleases in the pathway can act.
Following this initial processing step, a suite of ribonucleases cut down the 5' and 3' ends to yield the final, processed tRNA.
Although this processing pathway can function with as a few as one of its constituent exonucleases, the final tRNA product may be "imperfect," with a 3' end that may be longer or shorter than normal.
Unification Links: EcoCyc:PWY0-1479
Afonyushkin05: Afonyushkin T, Vecerek B, Moll I, Blasi U, Kaberdin VR (2005). "Both RNase E and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB." Nucleic Acids Res 33(5);1678-89. PMID: 15781494
AitBara10: Ait-Bara S, Carpousis AJ (2010). "Characterization of the RNA degradosome of Pseudoalteromonas haloplanktis: conservation of the RNase E-RhlB interaction in the gammaproteobacteria." J Bacteriol 192(20);5413-23. PMID: 20729366
Alifano94: Alifano P, Rivellini F, Piscitelli C, Arraiano CM, Bruni CB, Carlomagno MS (1994). "Ribonuclease E provides substrates for ribonuclease P-dependent processing of a polycistronic mRNA." Genes Dev 8(24);3021-31. PMID: 8001821
Ando01: Ando T, Tanaka T, Hori Y, Sakai E, Kikuchi Y (2001). "Human tyrosine tRNA is also internally cleavable by E. coli ribonuclease P RNA ribozyme in vitro." Biosci Biotechnol Biochem 65(12);2798-801. PMID: 11826982
Ando02: Ando T, Tanaka T, Hori Y, Kikuchi Y (2002). "Kinetics of hyperprocessing reaction of human tyrosine tRNA by ribonuclease P ribozyme from Escherichia coli." Biosci Biotechnol Biochem 66(9);1967-71. PMID: 12400701
Ando03: Ando T, Tanaka T, Kikuchi Y (2003). "Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes." Biosci Biotechnol Biochem 67(8);1825-7. PMID: 12951523
Ando03a: Ando T, Tanaka T, Kikuchi Y (2003). "Substrate shape specificity of E coli RNase P ribozyme is dependent on the concentration of magnesium ion." J Biochem (Tokyo) 133(4);445-51. PMID: 12761291
Apirion78: Apirion D (1978). "Isolation, genetic mapping and some characterization of a mutation in Escherichia coli that affects the processing of ribonuleic acid." Genetics 90(4);659-71. PMID: 369943
Apirion80a: Apirion D (1980). "Genetic mapping and some characterization of the rnpA49 mutation of Escherichia coli that affects the RNA-processing enzyme ribonuclease P." Genetics 94(2);291-9. PMID: 6156104
Arraiano88: Arraiano CM, Yancey SD, Kushner SR (1988). "Stabilization of discrete mRNA breakdown products in ams pnp rnb multiple mutants of Escherichia coli K-12." J Bacteriol 170(10);4625-33. PMID: 2459106
Asha83: Asha PK, Blouin RT, Zaniewski R, Deutscher MP (1983). "Ribonuclease BN: identification and partial characterization of a new tRNA processing enzyme." Proc Natl Acad Sci U S A 80(11);3301-4. PMID: 6344080
Babitzke91: Babitzke P, Kushner SR (1991). "The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli." Proc Natl Acad Sci U S A 88(1);1-5. PMID: 1846032
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