PathBank

Pathway Description

Protein Synthesis: Methionine

Rattus norvegicus

Category:

Protein Pathway

Sub-Categories:

Created: 2018-09-10

Last Updated: 2019-08-16

Protein synthesis is an essential life process that builds the important large amino acid macromolecules that function as enzymes, antibodies, and cellular structural components. Although synthesis begins with the transcription of DNA into RNA, this pathway depicts the reactions that occur during translation. Transcribed messenger RNA (mRNA), which contains the genetic code to direct protein synthesis, is transported out of the nucleus and becomes bound to ribosomes in the cytoplasm or endoplasmic reticulum. The amino acids required to assemble polypeptide chains are delivered to the ribosomes using transfer RNA (tRNA). Each tRNA molecule has both a binding site for a specific amino acid and a three-nucleotide sequence called the anticodon that forms three complementary base pairs with an mRNA codon. Charging or loading the appropriate amino acid onto its tRNA is carried out by an aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase. This enzyme catalyzes the esterification of an amino acid to one of all its compatible tRNAs to form an aminoacyl-tRNA. Each of the twenty amino acids has a corresponding aa-tRNA made by a specific aminoacyl-tRNA synthetase. Ribosomes match the anticodons of the charged tRNA molecules with successive codons of the mRNA. After a match is found, the ribosome transfers the amino acid from the matching tRNA onto the growing peptide chain via a reaction termed peptide condensation, and the tRNAs, no longer carrying amino acids, are released.

References

Protein Synthesis: Methionine References

Kuwano Y, Wool IG: The primary structure of rat ribosomal protein L3. Biochem Biophys Res Commun. 1992 Aug 31;187(1):58-64. doi: 10.1016/s0006-291x(05)81458-5.

Pubmed: 1520347

Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. doi: 10.1101/gr.2596504.

Pubmed: 15489334

Otaka E, Higo K, Itoh T: Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from Schizosaccharomyces pombe. Mol Gen Genet. 1983;191(3):519-24. doi: 10.1007/bf00425772.

Pubmed: 6355773

Chan YL, Olvera J, Wool IG: The primary structures of rat ribosomal proteins L4 and L41. Biochem Biophys Res Commun. 1995 Sep 25;214(3):810-8. doi: 10.1006/bbrc.1995.2359.

Pubmed: 7575549

Dresios J, Aschrafi A, Owens GC, Vanderklish PW, Edelman GM, Mauro VP: Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis. Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):1865-70. doi: 10.1073/pnas.0409764102. Epub 2005 Jan 31.

Pubmed: 15684048

Lundby A, Secher A, Lage K, Nordsborg NB, Dmytriyev A, Lundby C, Olsen JV: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun. 2012 Jun 6;3:876. doi: 10.1038/ncomms1871.

Pubmed: 22673903

Chan YL, Lin A, McNally J, Wool IG: The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA. J Biol Chem. 1987 Sep 15;262(26):12879-86.

Pubmed: 3624282

Tamura S, Kuwano Y, Nakayama T, Tanaka S, Tanaka T, Ogata K: Molecular cloning and nucleotide sequence of cDNA specific for rat ribosomal protein L5. Eur J Biochem. 1987 Oct 1;168(1):83-7. doi: 10.1111/j.1432-1033.1987.tb13390.x.

Pubmed: 3117543

Chan YL, Wool IG: The primary structure of rat ribosomal protein L6. Biochem Mol Biol Int. 1996 Jun;39(3):431-8.

Pubmed: 8828793

Wittmann-Liebold B, Geissler AW, Lin A, Wool IG: Sequence of the amino-terminal region of rat liver ribosomal proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and L39. J Supramol Struct. 1979;12(4):425-33. doi: 10.1002/jss.400120403.

Pubmed: 398910

Nakamura H, Tanaka T, Ishikawa K: Nucleotide sequence of cloned cDNA specific for rat ribosomal protein L7a. Nucleic Acids Res. 1989 Jun 26;17(12):4875.

Pubmed: 2748341

Lin A, Chan YL, McNally J, Peleg D, Meyuhas O, Wool IG: The primary structure of rat ribosomal protein L7. The presence near the amino terminus of L7 of five tandem repeats of a sequence of 12 amino acids. J Biol Chem. 1987 Sep 15;262(26):12665-71.

Pubmed: 3624274

Chan YL, Olvera J, Wool IG: The primary structures of rat ribosomal proteins: the characterization of the cDNAs for S21 and L39, corrections in the sequences of L7 and L18a, and the identification of L33. Biochem Biophys Res Commun. 1995 Aug 24;213(3):1042-50. doi: 10.1006/bbrc.1995.2233.

Pubmed: 7654221

Chan YL, Wool IG: The primary structure of rat ribosomal protein L8. Biochem Biophys Res Commun. 1992 Jun 15;185(2):539-47. doi: 10.1016/0006-291x(92)91658-d.

Pubmed: 1610349

Suzuki K, Olvera J, Wool IG: The primary structure of rat ribosomal protein L9. Gene. 1990 Sep 14;93(2):297-300. doi: 10.1016/0378-1119(90)90239-n.

Pubmed: 2227441

Olvera J, Wool IG: The primary structure of rat ribosomal protein L10a. Biochem Biophys Res Commun. 1996 Mar 27;220(3):954-7. doi: 10.1006/bbrc.1996.0513.

Pubmed: 8607874

Chan YL, Diaz JJ, Denoroy L, Madjar JJ, Wool IG: The primary structure of rat ribosomal protein L10: relationship to a Jun-binding protein and to a putative Wilms' tumor suppressor. Biochem Biophys Res Commun. 1996 Aug 23;225(3):952-6. doi: 10.1006/bbrc.1996.1277.

Pubmed: 8780716

Chan YL, Olvera J, Paz V, Wool IG: The primary structure of rat ribosomal protein L11. Biochem Biophys Res Commun. 1992 May 29;185(1):356-62. doi: 10.1016/s0006-291x(05)80993-3.

Pubmed: 1599472

This pathway was propagated using PathWhiz - Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.

Propagated from SMP0111875

Highlighted elements will appear in red.

Highlight Compounds

	Adenosine monophosphate
	Adenosine triphosphate
	L-Methionine
	Pyrophosphate

Highlight Proteins

	40S ribosomal protein S2
	40S ribosomal protein S3
	60S ribosomal protein L3
	Methionyl-tRNA synthetase

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