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• hydroxyproline The hydroxylation of prolyl and lysyl side chains in procollagen requires ascorbic acid (vitamin C). As a result patients with vitamin C deficiency (scurvy) form a collagen with insufficient hydroxyproline that denatures spontaneously at room temperature. Prolonged deficiency of vitamin C causes scurvy (i.e. gingival inflammation and bleeding gums, dry mouth and eyes, bruising, fatigue). Collagen accounts for approximately 25% of the body protein in adults and 15% to 20% in children. It is most abundant in strong, tough connective tissues. Type I collagen is by far the most abundant collagen in the body. It has a most unusual amino acid composition, with 33% glycine and 10% proline . It also contains hydroxyproline and hydroxylysine . The basic structural unit of collagen fibrils, the tropocollagen molecule, consists of three intertwined polypeptides. In the case of type I collagen, it has a very unusual amino acid sequence, with glycine in every third position. Tropocollagen is the longest known protein and is formed from procollagen, which is secreted by fibroblasts . The three helical polypeptides of the tropocollagen molecule are wound around each other in a right-handed triple helix. Note: The long, ropelike tropocollagen molecules form fibrils by aligning themselves in parallel. Once secreted outside the cell tropocollagen units are crosslinked through covalent bonding between adjacent lysine residues to produce mature collagen. Remember: Vitamin C influences the formation of collagen, which is the organic matrix found in dentin and cementum (see note #1 below). 1. Hydroxyproline and hydroxylysine are nonstandard amino acids that are present in Notes few other proteins. For this reason, their concentration in a particular tissue is a good estimate of the collagen content as well. They are not used directly in the reactions of protein synthesis. These amino acids are formed by the hydroxylation of proline and lysine (by lysyl hydroxylase). This hydroxylation involves α-keto- glutarate, oxygen, Fe 2+ and vitamin C (ascorbic acid), which is required because it restores iron to its reduced state (Fe 2+ ). 2. Collagen and reticular fibers make up the stroma of all lymphoid tissues except the thymus..

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Hydroxylation of the Eukaryotic Ribosomal Decoding Center Affects Translational Accuracy
Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy Christoph Loenarza,1, Rok Sekirnika,2, Armin Thalhammera,2, Wei Gea, Ekaterina Spivakovskya, Mukram M. Mackeena,b,3, Michael A. McDonougha, Matthew E. Cockmanc, Benedikt M. Kesslerb, Peter J. Ratcliffec, Alexander Wolfa,4, and Christopher J. Schofielda,1 aChemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, Oxford OX1 3TA, United Kingdom; bTarget Discovery Institute, University of Oxford, Oxford OX3 7FZ, United Kingdom; and cCentre for Cellular and Molecular Physiology, University of Oxford, Oxford OX3 7BN, United Kingdom Edited by William G. Kaelin, Jr., Harvard Medical School, Boston, MA, and approved January 24, 2014 (received for review July 31, 2013) The mechanisms by which gene expression is regulated by oxygen Enzyme-catalyzed hydroxylation of intracellularly localized are of considerable interest from basic science and therapeutic proteins was once thought to be rare, but accumulating recent perspectives. Using mass spectrometric analyses of Saccharomyces evidence suggests it is widespread (11). Motivated by these cerevisiae ribosomes, we found that the amino acid residue in findings, we investigated whether the translation of mRNA to closest proximity to the decoding center, Pro-64 of the 40S subunit protein is affected by oxygen-dependent modifications. A rapidly ribosomal protein Rps23p (RPS23 Pro-62 in humans) undergoes growing eukaryotic cell devotes most of its resources to the tran- posttranslational hydroxylation. We identify RPS23 hydroxylases scription, splicing, and transport of ribosomal proteins and rRNA as a highly conserved eukaryotic subfamily of Fe(II) and 2-oxoglu- (12). We therefore reasoned that ribosomal modification is a tarate dependent oxygenases; their catalytic domain is closely re- candidate mechanism for the regulation of protein expression.
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J Clin Pathol: first published as 10.1136/jcp.s3-12.1.49 on 1 January 1978. Downloaded from J. clin. Path., 31, Suppl. (Roy. Coll. Path.), 12, 49-58 Collagen and elastin fibres A. J. BAILEY From the Agricultural Research Council, Meat Research Institute, Langford, Bristol Although an understanding of the intracellular native collagen was generated from type I pro- biosynthesis of both collagen and elastin is of collagen. Whether this means that the two pro- considerable importance it is the subsequent extra- collagens are converted by different enzyme systems cellular changes involving fibrogenesis and cross- and the type III enzyme was deficient in these linking that ensure that these proteins ultimately fibroblast cultures, or that the processing of pro become the major supporting tissues of the body. type III is extremely slow, is not known. The latter This paper summarises the formation and stability proposal is consistent with the higher proportion of collagen and elastin fibres. of soluble pro type III extractable from tissue (Lenaers and Lapiere, 1975; Timpl et al., 1975). Collagen Basement membrane collagens, on the other hand, do not form fibres and this property may be The non-helical regions at the ends of the triple due to the retention of the non-helical extension helix of procollagen probably provide a number of peptides (Kefalides, 1973). In-vivo biosynthetic different intracellular functions-that is, initiating studies showing the absence of any extension peptide rapid formation of the triple helix; inhibiting intra- removal support this (Minor et al., 1976), but other cellular fibrillogenesis; and facilitating transmem- workers have reported that there is some cleavage brane movement.
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