[14] Amino-terminal acetylation of proteins: An overview

Tsunasawa, Susumu; Sakiyama, Fumio

doi:10.1016/0076-6879(84)06016-x

Cited by 93 publications

(34 citation statements)

References 30 publications

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“…In isolated cases, such as f-endorphin (25) and a-melanocyte-stimulating hormone (26), N-terminal acetylation directly affects activity. A possible protective role against proteolysis has been debated (27). N-terminal proteolytic processing and acetylation in the LS of RbuP2 carboxylase may be related to holoenzyme assembly, perhaps as a prerequisite for association with a chloroplastic chaperonin (28), although other functions are equally possible.…”

Section: Discussionmentioning

confidence: 99%

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Houtz

Stults

Mulligan

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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Two adjacent N-terminal tryptic peptides of the large subunit of ribulose bisphosphate carboxylase/oxygenase [3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] from spinach, wheat, tobacco, and muskmelon were removed by limited tryptic proteolysis. Characterization by peptide sequencing, amino acid composition, and tandem mass spectrometry revealed that the N-terminal residue from the large subunit of the enzyme from each plant species was acetylated proline. The sequence of the penultimate N-terminal tryptic peptide from the large subunit of the spinach and wheat enzyme was consistent with previous primary structure determinations. However, the penultimate N-terminal peptide from the large subunit of both the tobacco and muskmelon enzymes, while identical, differed from the corresponding peptide from spinach and wheat by containing a trimethyllysyl residue at position 14. Thus, tryptic proteolysis occurred at lysine-18 rather than lysine-14 as with the spinach and wheat enzymes. A comparison of the DNA sequences for the large subunit of ribulose bisphosphate carboxylase/oxygenase indicates that the N terminus has been post-translationally processed by removal of methionine-1 and serine-2 followed by acetylation of proline-3. In addition, for the enzyme from tobacco and muskmelon a third post-translational modification occurs at lysine-14 in the form of NE-trimethylation.Ribulose bisphosphate carboxylase/oxygenase [RbuP2 carboxylase, 3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] is a hexadecameric plant protein with eight large subunits (LSs) and eight small subunits (SSs) (for a recent review, see ref.

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Section: Discussionmentioning

confidence: 99%

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Houtz

Stults

Mulligan

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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“…Cold Spring Harbor Laboratory Press on May 11, 2018 -Published by genesdev.cshlp.org Downloaded from stood, amino-terminal acetylation is thought primarily to increase protein stability rather than to alter gene expression (Tsunasawa and Sakiyama 1984).…”

Section: Genes and Developmentmentioning

confidence: 99%

Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.

Braunstein¹,

Rose²,

Holmes³

et al. 1993

Genes Dev.

764

542

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Two classes of sequences in the yeast Saccharomyces cerevisiae are subject to transcriptional silencing: the silent mating-type cassettes and telomeres. In this report we demonstrate that the silencing of these regions is strictly associated with acetylation of the e-amino groups of lysines in the amino-terminal domains of three of the four core histones. Both the silent mating-type cassettes and the Y domains of telomeres are packaged in nucleosomes in vivo that are hypoacetylated relative to those packaging active genes. This difference in acetylation is eliminated by genetic inactivation of silencing: The silent cassettes from sir2, sir3, or sir4 cells show the same level of acetylation as other active genes. The correspondence of silencing and hypoacetylation of the mating-type cassettes is observed even for an allele lacking a promoter, indicating that silencing per se, rather than the absence of transcription, is correlated with hypoacetylation. Finally, overexpression of Sir2p, a protein required for transcriptional silencing in yeast, yields substantial histone deacetylation in vivo. These studies fortify the hypothesis that silencing in yeast results from heterochromatin formation and argue that the silencing proteins participate in this formation.

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“…Glutamine can spontaneously cyclize to block the N terminus of Sendai virus F0, but an Nterminal isoleucine on NDV F0 would not. Acetylation is the commonest blocking modification at the N termini of proteins in eukaryotic cells, but is normally considered a modification of proteins in the cytosol and is not known to occur at N-terminal isoleucine (Tsunasawa & Sakiyama, 1984). Acetylation can, however, occur in the endoplasmic reticulum and secretory granules of rat pituitary cells (Glembotski, 1982).…”

Section: Sv$ ~: Hrq~d T ¥~ a I T S Ast S ~Lsmentioning

confidence: 99%

Nucleotide Sequence of the Gene Encoding the Fusion Glycoprotein of Newcastle Disease Virus

Chambers

Millar

Emmerson

1986

Journal of General Virology

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SUMMARYThe nucleotide sequence of the gene encoding the fusion (F) glycoprotein of the Beaudette C strain of Newcastle disease virus (NDV) has been determined from cDNA clones obtained from virion RNA. The gene is 1792 nucleotides long, including mRNA start and polyadenylation signals typical of paramyxoviruses. The single open reading frame encodes a polypeptide of 553 amino acids, with a predicted molecular weight of 59042. The F polypeptide has three regions of high hydrophobicity: an Nterminal signal peptide, the N terminus of F~ (known from protein sequencing) and a C-terminal membrane-spanning region by which the F glycoprotein is anchored to the membrane. The cleavage site of F0 is located in a highly basic region of the F polypeptide. Five potential asparagine-linked glycosylation sites are present in the amino acid sequence, of which one is in Fz and the others in F~. Comparison of the NDV F amino acid sequence to those from other paramyxoviruses reveals homology to Sendai virus, simian virus 5 and human respiratory syncytial virus. There is also limited homology between the N terminus ofF1 of NDV and the N termini of HA2 of influenza viruses. Post-translational modifications of the NDV F polypeptide are discussed in the light of information provided by the amino acid sequence.

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[14] Amino-terminal acetylation of proteins: An overview

Cited by 93 publications

References 30 publications

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.

Nucleotide Sequence of the Gene Encoding the Fusion Glycoprotein of Newcastle Disease Virus

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