In Vivo Chemical Modification of Proteins (Post-Translational Modification)

Wold, Finn

doi:10.1146/annurev.bi.50.070181.004031

Cited by 478 publications

(181 citation statements)

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“…3). The high proportion of lysine residues both within and outside the repeats calls to mind the case of the connective tissue structural proteins collagen and elastin, in which lysines are subject to posttranslational modification and serve as sites of intra-and intermolecular cross-links (27).…”

Section: Resultsmentioning

confidence: 99%

An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis

et al. 1995

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We describe the identification and characterization of a gene, herein designated cotG, encoding an abundant coat protein from the spores of Bacillus subtilis. The cotG open reading frame is 195 codons in length and is capable of encoding a polypeptide of 24 kDa that contains nine tandem copies of the 13-amino-acid long, approximately repeated sequence H/Y-K-K-S-Y-R/C-S/T-H/Y-K-K-S-R-S.cotG is located at 300؇ on the genetic map close to another coat protein gene, cotB. The cotG and cotB genes are in divergent orientation and are separated by 1.3 kb. Like the promoter for cotB, the cotG promoter is induced at a late stage of sporulation under the control of the RNA polymerase sigma factor K and the DNA-binding protein GerE. The ؊10 and ؊35 nucleotide sequences of the cotG promoter resemble those of other promoters recognized by K -containing RNA polymerase, and centered 70 bp upstream of the apparent start site is a sequence that matches the consensus binding site for GerE. Spore coat proteins from a newly constructed cotG null mutant lack not only CotG but also CotB, a finding that suggests that CotG may be a morphogenetic protein that is required for the incorporation of CotB into the coat.Spores of the gram-positive bacterium Bacillus subtilis are encased in a complex protein shell known as the coat consisting of 15 or more different proteins. So far, genes for 10 of these coat proteins have been identified. These are located at diverse positions on the chromosome and encode polypeptides of 65 (CotA), 59 (CotB), 10 (CotC), 9 (CotD), 24 (CotE), 19 (CotF), 10 (CotT), 19 (CotX), 26 (CotY), and 18 (CotZ) kDa (2,4,7,29,31). In the cases of CotF and CotT, little of the full-length gene products is found in the coat. Rather, CotF is present as two proteolytic fragments of 8 and 5 kDa, and CotT is present as a proteolytic fragment of 8 kDa (2, 4). Coat proteins are organized in two principal layers, a lamellar inner coat and an electron-dense outer coat (1), with certain proteins, such as CotD, being present in the inner coat, and other proteins, such as CotA, CotB, and CotC, being present in the outer coat (31). The coat is assembled at intermediate to late stages of sporulation when the nascent spore (known as the forespore) is present as a free protoplast, wholly engulfed within the mother cell compartment of the developing sporangium. Coat proteins are recruited to the outer surface of the membrane surrounding the forespore by the sporulation protein SpoIVA (which has not been detected in mature spores and hence is not referred to as a coat protein) (8,19,21). Morphogenetic events under the control of SpoIVA lead to the assembly of a ring of CotE protein around the forespore (8). The CotE ring is separated from the outer surface of the forespore (where SpoIVA is located) by a small gap, which is believed to be the site at which the inner coat will be assembled. Meanwhile, CotE dictates the assembly of the proteins of the outer coat, where it is itself located (8, 31). The production of coat proteins is governed by ...

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Section: Resultsmentioning

confidence: 99%

An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis

et al. 1995

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“…Post-transcriptional modifications of enzymes are well-known and many examples of covalent attachments of chemical groups on amino acid sidechains are described [11]. Only a few cases of modifications of aminoacyl-tRNA synthetases have been reported [12][13][14][15].…”

Section: Resultsmentioning

confidence: 99%

Covalent attachment of aspartic acid to yeast aspartyl‐tRNA synthetase induced by the enzyme

et al. 1982

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Aspartic acid can be covalently linked to yeast aspartyl-tRNA synthetase and to other proteins, in the absence of tRNA, under conditions where the synthetase activates the amino acid into aspartyl-adenylate, i.e., in the presence of ATP and MgC12. The linkage between aspartic acid and the protein is acid and alkali resistant; thus it is likely a peptide-like amide bond formed between the activated carboxylate group of aspartic acid and the,primary amine function of the side chain of lysine residues.Aminoacyl-tRNA synthetase

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“…However, glutamic acid, and not glutamine, was predicted by cDNA sequencing for GPIIbP in HEL and in megakaryocyte cells [7,12,22]. The most likely explanations for the discrepancy between the cDNA-predicted and the chemically established C-terminal residue for GPIIb@ are either that there are cell-type specific copies of the exon coding for the C-terminal, or that the C-terminus of the GPIIb precursor is posttr~slationally modified, as already observed in other proteins [23]. Recently, Prandini et al [24] have sequenced the 3 ' end of the GPIIb gene from a genomic library, containing an exon encoding the 19 C-terminal amino acid residues of GPIIb and a 3 ' untranslated region; the sequence showed glutamic acid as the C-terminal residue.…”

Section: Fully Reduced and Carboxymethylatedmentioning

confidence: 99%

C‐terminal amino acid determination of the transmembrane subunits of the human platelet fibrinogen receptor, the GPIIb/IIIa complex

1990

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Glycoproteins IIb (GPIIb) and IIIa (GPIIIa) form the Ca2+ ‐dependent GPIIb/IIIa complex, which acts as the fibrinogen receptor on activated platelets. GPIIb and GPIIIa are synthesized as single peptide chains. The GPIIb precursor is processed proteolytically to yield two disulphide‐bonded chains, GPIIba and GPIIbß. The GPIIb/IIIa complex has two membrane attachment sites located at the C‐tennini ofGPIIß and GPIIIa. The short cytoplasmic tails of GPIIbß and/or GPIIIa become most likely associated to the cytoskeleton of activated platelets. In the present work the C‐tenninal amino acid residues of platelet GPIIbß and GPIIIa have been analyzed by protein‐chemical methods and compared with those predicted from cDNA analysis. We were able to confirm the positions of the C‐tennini in both glycoproteins and the identity of the C‐tenninus predicted for GPIIIa, i.e. threonine. However, glutamine, not glutamic acid as predicted for GPIIbß from the human erythroleukemic cell line and megakaryocyte cells, was found to be the C‐terminal amino acid of GPIIß. This indicates that the glutamic arid in the GPIIb precursor is posttranslationally modified to glutamine.

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In Vivo Chemical Modification of Proteins (Post-Translational Modification)

Cited by 478 publications

References 0 publications

An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis

An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis

Covalent attachment of aspartic acid to yeast aspartyl‐tRNA synthetase induced by the enzyme

C‐terminal amino acid determination of the transmembrane subunits of the human platelet fibrinogen receptor, the GPIIb/IIIa complex

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