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Pathway Description
Protein Synthesis: Threonine
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Created: 2018-09-10
Last Updated: 2019-09-13
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: Threonine References
Duga S, Asselta R, Malcovati M, Tenchini ML, Ronchi S, Simonic T: The intron-containing L3 ribosomal protein gene (RPL3): sequence analysis and identification of U43 and of two novel intronic small nucleolar RNAs. Biochim Biophys Acta. 2000 Feb 29;1490(3):225-36. doi: 10.1016/s0167-4781(99)00237-7.
Pubmed: 10684968
Simonic T, Gaudi S, Giussani F, Malcovati M, Ronchi S, Tenchini ML: cDNA sequence for bovine ribosomal protein L3 carrying a bipartite nuclear targeting motif, identified also in many other ribosomal proteins. Biochim Biophys Acta. 1994 Nov 22;1219(3):706-10. doi: 10.1016/0167-4781(94)90232-1.
Pubmed: 7948030
Harhay GP, Sonstegard TS, Keele JW, Heaton MP, Clawson ML, Snelling WM, Wiedmann RT, Van Tassell CP, Smith TP: Characterization of 954 bovine full-CDS cDNA sequences. BMC Genomics. 2005 Nov 23;6:166. doi: 10.1186/1471-2164-6-166.
Pubmed: 16305752
Green H, Canfield AE, Hillarby MC, Grant ME, Boot-Handford RP, Freemont AJ, Wallis GA: The ribosomal protein QM is expressed differentially during vertebrate endochondral bone development. J Bone Miner Res. 2000 Jun;15(6):1066-75. doi: 10.1359/jbmr.2000.15.6.1066.
Pubmed: 10841175
Ishiwata H, Katsuma S, Kizaki K, Patel OV, Nakano H, Takahashi T, Imai K, Hirasawa A, Shiojima S, Ikawa H, Suzuki Y, Tsujimoto G, Izaike Y, Todoroki J, Hashizume K: Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray. Mol Reprod Dev. 2003 May;65(1):9-18. doi: 10.1002/mrd.10292.
Pubmed: 12658628
Zimin AV, Delcher AL, Florea L, Kelley DR, Schatz MC, Puiu D, Hanrahan F, Pertea G, Van Tassell CP, Sonstegard TS, Marcais G, Roberts M, Subramanian P, Yorke JA, Salzberg SL: A whole-genome assembly of the domestic cow, Bos taurus. Genome Biol. 2009;10(4):R42. doi: 10.1186/gb-2009-10-4-r42. Epub 2009 Apr 24.
Pubmed: 19393038
Su S, Bird RC: Cell cycle, differentiation and tissue-independent expression of ribosomal protein L37. Eur J Biochem. 1995 Sep 15;232(3):789-97.
Pubmed: 7588717
Schlesinger DH, Goldstein G, Niall HD: The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells. Biochemistry. 1975 May 20;14(10):2214-8. doi: 10.1021/bi00681a026.
Pubmed: 1170880
Hamilton JW, Rouse JB: The biosynthesis of ubiquitin by parathyroid gland. Biochem Biophys Res Commun. 1980 Sep 16;96(1):114-20. doi: 10.1016/0006-291x(80)91188-2.
Pubmed: 6254502
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 SMP0119302
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