The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Analysis of myristic acid analogs containing oxygen, sulfur, double bonds, triple bonds, and/or an aromatic residue

Kishore, Nandini S.; Lu, Taotao; Knoll, Laura J.; Katoh, Akira; Rudnick, David A.; Mehta, Pramod P.; Devadas, Balekudru; Huhn, Meik; Atwood, J L; Adams, Steven P.

doi:10.1016/s0021-9258(18)31523-0

Cited by 89 publications

(21 citation statements)

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“…N-Myristoyltransferase (NMT) is an eukaryotic enzyme devoted to catalyzing the acylation with myristic acid (using myristoyl-CoA as the activated reagent) of the alphaamine group of proteins exposed at the N-terminus of the NMT recognition sequence Gly-X1-X2-X3-Ser/Thr (Lys) (X is any amino acid) (Figure 6d). NMT can also use surrogates of the myristic acid as a substrate [108][109][110] such as azido or alkyne containing fatty acids, allowing the N-terminal site-specific introduction of an orthogonal reactive handle that can be conveniently exploited for protein decoration using Staudinger ligation [111], CuAAC, or strain-promoted azide-alkyne cycloaddition (SPAAC) click-chemistries [50,112,113]. A protocol for the recombinant co-expression in Escherichia coli of NMT and the protein target for the in vivo N-terminal labeling with a clickable myristic acid analog was also provided [114].…”

Section: N-myristoyltransferasementioning

confidence: 99%

Exploiting Protein N-Terminus for Site-Specific Bioconjugation

et al. 2021

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Although a plethora of chemistries have been developed to selectively decorate protein molecules, novel strategies continue to be reported with the final aim of improving selectivity and mildness of the reaction conditions, preserve protein integrity, and fulfill all the increasing requirements of the modern applications of protein conjugates. The targeting of the protein N-terminal alpha-amine group appears a convenient solution to the issue, emerging as a useful and unique reactive site universally present in each protein molecule. Herein, we provide an updated overview of the methodologies developed until today to afford the selective modification of proteins through the targeting of the N-terminal alpha-amine. Chemical and enzymatic strategies enabling the selective labeling of the protein N-terminal alpha-amine group are described.

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Section: N-myristoyltransferasementioning

confidence: 99%

Exploiting Protein N-Terminus for Site-Specific Bioconjugation

et al. 2021

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“…The second step involves addition of purified NMT (Rudnick et al, 1990) together with an octapeptide containing residues 2-9 of the candidate sequence. The enzymatically generated acylpeptide is purified from the reaction mixture by reverse phase HPLC and detected by an in-line scintillation counter (Kishore et al ., 1991) .…”

Section: Immunocytochemical Studiesmentioning

confidence: 99%

“…Note that (a) the intensity of ['H]palmitate labeled bands in whole cell lysates was markedly reduced after treatment with hydroxylamine compared to Tris (data not shown ; see text) and (b) that in the Tristreated gel, no radiolabeled proteins were detected after immunoprecipitation of [3H]palmitate-labeled HT29/ino cell lysates (data not shown) . substrates for NMT (Heuckeroth et al ., 1988;Heuckeroth and Gordon, 1989;Bryant et al ., 1991 ;Kishore et al ., 1991) .…”

Section: Immunologic Studies Of Isa Accumulation/targeting In Cultured Human Intestinal Cell Linesmentioning

confidence: 99%

A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin.

Wice

Gordon

1992

The Journal of Cell Biology

101

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Abstract. The human intestinal epithelium is rapidly and perpetually renewed as the descendants of multipotent stem cells located in crypts undergo proliferation, differentiation, and eventual exfoliation during a very well organized migration along the crypt to villus axis. The mechanisms that establish and maintain this balance between proliferation and differentiation are largely unknown . We have utilized HT29 cells, derived from a human colon adenocarcinoma, as a model system for identifying gene products that may regulate these processes . Proliferating HT-29 cells cultured in the absence of glucose (e.g., using inosine as the carbon source) have some of the characteristics of undifferentiated but committed crypt epithelial cells while postconfluent cells cultured in the absence of glucose resemble terminally differentiated enterocytes or goblet cells . A cDNA library, constructed from exponentially growing HT-29 cells maintained in inosine-containing media, was sequentially screened with a series of probes depleted of sequences encoding housekeeping functions and enriched for intestine-specific sequences that are expressed in proliferating committed, but not differentiated, epithelial cells. Of 100,000 recombinant phage surveyed, one was found whose cDNA was derived from an apparently gut-specific mRNA.

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“…The myristic acid analog 6-oxatetradecanoate (06) was used to further explore the effect of Faalp on nmt1181 strains . Substitution of oxygen for methylene at C6 (the carboxyl carbon = Cl) produces an analog whose chain length and bond geometry are similar to those of myristate but whose hydrophobicity is equivalent to dodecanoic acid (C12 :0) (Heuckeroth et al, 1988;Kishore et al, 1991). 06 is a substrate for S. cerevisiae NMT in vitro (Heuckeroth et al ., 1988;Kishore et al ., 1991) .…”

Section: Withmentioning

confidence: 99%

“…Myristate and palmitate were purchased from NuCheck Prep (Elysian, MN) . 06 was synthesized as in Kishore et al . (1991) .…”

Section: Strains and Mediamentioning

confidence: 99%

Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation.

Duronio

Knoll

Gordon

1992

The Journal of Cell Biology

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Regulation of myristoylCoA pools in Saccharomyces cerevisiae plays an important role in modulating the activity of myristoylCoA:protein N-myristoyltransferase (NMT), an essential enzyme with an ordered Bi Bi reaction that catalyzes the transfer of myristate from myristoylCoA to greater than or equal to 12 cellular proteins. At least two pathways are available for generating myristoylCoA: de novo synthesis by the multifunctional, multisubunit fatty acid synthetase complex (FAS) and activation of exogenous myristate by acylCoA synthetase. The FAA1 (fatty acid activation) gene has been isolated by genetic complementation of a faal mutant. This single copy gene, which maps to the right arm of chromosome XV, specifies a long chain acylCoA synthetase of 700 amino acids. Analyses of strains containing NMT1 and a faal null mutation indicated that FAA1 is not essential for vegetative growth when an active de novo pathway for fatty acid synthesis is present. The role of FAA1 in cellular lipid metabolism and protein N-myristoylation was therefore assessed in strains subjected to biochemical or genetic blockade of FAS. At 36 degrees C, FAA1 is required for the utilization of exogenous myristate by NMT and for the synthesis of several phospholipid species. This requirement is not apparent at 24 or 30 degrees C, suggesting that S. cerevisiae contains another acylCoA synthetase activity whose chain length and/or temperature optima may differ from Faalp.

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The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Analysis of myristic acid analogs containing oxygen, sulfur, double bonds, triple bonds, and/or an aromatic residue

Cited by 89 publications

References 1 publication

Exploiting Protein N-Terminus for Site-Specific Bioconjugation

Exploiting Protein N-Terminus for Site-Specific Bioconjugation

A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin.

Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation.

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