Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c. The specificities of methionine aminopeptidase and acetyltransferase.
Journal of Biological ChemistryPublished 1 May 1985Open access
Susumu Tsunasawa, John Stewart, Fred Sherman
Citations241
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SJR score1.71
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TL;DR
Yeast contains acetyltransferases that acetylates these mutant forms of iso-1-cytochromes c because their amino-terminal regions resemble the amino- terminal regions of natural occurring proteins which are normally acetylated.
Abstract
Met-Ile-Glu-Phe-Lys- Met-Asn-Lys-Phe-Lys-Ala
Keywords
Materials ScienceMedicineBiochemistry, Genetics and Molecular Biology
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95 Citations1979Richard Firtel, Roxana Timm +2 more
The nucleotide sequences at the 5' end of one actin cDNA and six actin genomic clones from Dictyostelium have been determined and show strong conservation for six of the seven genes relative to the NH2-terminal region of Physarum actin.
Journal of Molecular BiologyThe protein subunit of turnip yellow mosaic virus
95 Citations1961J. Ieuan Harris, J. Roger Hindley
The protein shell of turnip yellow mosaic virus is shown to consist of identical “chemical” subunits each with a molecular weight of 20,000, and was found to contain four SH groups per subunit.
Nucleic Acids ResearchMolecular cloning and sequence analysis of adult chicken β globin cDNA
95 Citations1979Robert I. Richards, John Shine +3 more
Journal of Biological ChemistryMouse liver metallothioneins. Complete amino acid sequence of metallothionein-I.
93 Citations1977I.Y. Huang, Akira Yoshida
Automated sequence analysis of a major cyanogen bromide peptide consisting of 60 amino acid residues, as well as characterization of the peptides obtained from trypsin and papain digestion, led to the elucidation of the complete primary structure of this protein.
Methods in enzymology on CD-ROM/Methods in enzymology[14] Amino-terminal acetylation of proteins: An overview
91 Citations1984Susumu Tsunasawa, Fumio Sakiyama
Journal of Biological ChemistryComparison of Myoglobins from Harbor Seal, Porpoise, and Sperm Whale
90 Citations1969Ralph Bradshaw, Frank R.N. Gurd
The sharpest contrasts were obtained in the rates of denaturation by cupric ion, in which the whale protein was set apart in two respects, and its reaction rate was much more effectively depressed by addition of small quantities of phosphate.
Proceedings of the National Academy of SciencesNucleotide sequence of the thrA gene of Escherichia coli.
90 Citations1980Michaël Katinka, Pascale Cossart +6 more
The thrA gene of Escherichia coli codes for a single polypeptide chain having two enzymatic activities required for the biosynthesis of threonine, aspartokinase I and homoserine dehydrogenase I, and an internal sequence that resembles the structure of bacterial ribosome-binding sites suggests that the singlepolypeptides chain was formed by the fusion of two genes.
BiochemistryAmino Acid Sequence Studies on the Tryptic Peptides of the Coat Protein of the Bacteriophage R17<sup>*</sup>
89 Citations1967Klaus Weber
Nucleic Acids ResearchThe nucleotide sequence of the<i>Escherichta coli fus</i>gene, coding for elongation factor G
88 Citations1984Janice M. Zengel, Richard Archer +1 more
A comparison of the nucleotide and amino acid sequences of elongation factors G and Tu reveals a limited but significant homology between the two proteins within the 150 amino acid residues at their amino-terminal ends.
Nucleic Acids ResearchNucleotide sequence of cloned cDNA of human apolipoprotein A-l
87 Citations1983Peter Cheung, Lawrence Chan
ApoA-I is the major human HDL apoprotein and by oligonucleotide hybridization, 5 dscDNA clones to human hepatic apo A-I mRNA are isolated, which predicts a peptide sequence of 267 amino acids which is very similar to the sequence reported by Brewer et al, 1978.
BiochemistrySome sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase
87 Citations1980Jack R. Jabusch, David L. Farb +2 more
Human Cu-Zn superoxide dismutase prepared by different methods shows varying properties relevant to its sulfhydryl chemistry, and a cysteine residue not found in the analogous bovine enzyme appears to be responsible for its unusual lability.
CellNucleotide sequence of turnip yellow mosaic virus coat protein mRNA
86 Citations1978H. Guilley, Jean‐Paul Briand
The primary structure of the coat protein messenger RNA of turnip yellow mosaic virus is presented and the codon preference is particularly marked for Leu, lle Val, Thr and Cys.
Journal of Biological ChemistryStructure of the metJBLF cluster in Escherichia coli K12. Sequence of the metB structural gene and of the 5‘- and 3‘-flanking regions of the metBL operon.
86 Citations1983Nathalie Duchange, Mario M. Zakin +6 more
The overall organization of the metJBLF gene cluster is discussed and there is no structural evidence of a classical attenuation mechanism in the regulation of this operon coding for enzymes implicated in an amino acid biosynthetic pathway.
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