Acetyl nitrite: a useful nitrosating reagent

Kyte, A. B.; Jones-Parry, Richard; Whittaker, D.

doi:10.1039/c39820000074

Cited by 12 publications

(6 citation statements)

References 1 publication

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“…It reveals 12 hydrophobic segments of at least 20 amino [22], the CANl arginine permease (201 and the HIP1 histidine permeuse (211. Hydrophobicity (below the line) and hydrophilicity (above the line) values were determined using the Kyte and Doolittle algorithm [54]. They were obtained by averaging hydropathy values for a window of 15 residues acids presenting average hydropathy values lower than -1.3, which indicates that these segments might form membranespanning r-helices (see [43]).…”

Section: Hydroputhy Profilementioning

confidence: 99%

GAP1, the general amino acid permease gene of Saccharomyces cerevisiae

Jauniaux

Grenson

1990

European Journal of Biochemistry

271

170

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In Saccharomyces cerevisiae, mutations at the GAP1 locus selectively abolish the activity of the general amino acid transport system. This permease catalyses active transport of apparently all biological amino acids across the plasma membrane. We have determined the nucleotide sequence of the GAP1 gene. The sequence contains an open reading frame of 601 codons corresponding to a polypeptide of Mr 65578. This polypeptide is strongly hydrophobic; it exhibits three potential glycosylation sites. Hydropathy analysis suggests 12 membrane‐spanning regions. The N‐terminal domain is charged, it does not resemble hydrophobic signal sequences found in secreted proteins. Hence the GAP1 gene encodes a protein with characteristics typical of integral membrane proteins translocating ligants across cellular membranes. The deduced amino acid sequence of GAP1 protein presents strong similarities to those of the yeast arginine, histidine and proline permeases, suggesting a common evolutionary origin for these amino acid permeases. Nitrogen‐source regulation of the GAP1 permease is believed to occur at two distinct levels, i.e. permease synthesis and permease activity [Grenson (1983) Eur. J. Biochem. 133, 135–139]. Northern analysis of GAP1‐specific transcripts in wild‐type and in mutant strains is in agreement with these views and indicates that nitrogen catabolite repression of GAP1 synthesis occurs at the RNA level.

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Section: Hydroputhy Profilementioning

confidence: 99%

GAP1, the general amino acid permease gene of Saccharomyces cerevisiae

Jauniaux

Grenson

1990

European Journal of Biochemistry

271

170

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“…Regions with high G+C content were also sequenced in parallel with deazaguanosine and automated flume~cent DNA ~queneing (EMBL flaon.~,cent DNA sequencer, Heidell~rg, Germany). Analysi~ of the DNA sequence was conducted with the ald of the lntelliGenetics Suite version 5.4 (lntelh-Genetics Inc., Mountain View, CA), and the homology search was carried out on the Swi~s-Prot database The hydropathy plot wan produced by the method of Kyt¢ and Doolittle [21] w~th a w~dth of 9 residues,…”

Section: Edna Sequencing Attd Sequence Attalyatsmentioning

confidence: 99%

cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils

et al. 1992

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The fulldength eDNA of a neutrophil antibiotic dodecapeptide has been cloned by rever~e transenptmn/PCg from bovine bone marrow RNA.This peptlde was originally i~olated from bovine neutrophils, and shown to exert a potent antimicrobial activity in vitro on both l~nchertchia coil and Staphylococcus aureus. The eDNA codes for a polyrmptlde of 155 amino acid residues with a predicted mass of 17,629 Da and a pl or 8 03.The deduced sequence comprises a putative signal peptlde of 29 amino acids, a 114 residue pro-region, and a earboxy-lenninal dodecapeptide corresponding to the mature antibiotic. The pro-sequence displays extensive idenuty to corresponding regtons of other structurally unrelated anub~otic peptides of bovine neutrophils recently cloned.Ncutrophil; Antibiotic; Cyclic dodecapepude; eDNA 1, INTRODUCTIONA central role of neutrophils in the initial host response to microbial challenge is testified by a massive recruitment of" these cells at the infection site, followed by rapid and effective pathogen inactivation. Killing is ensured by the production of highly reactive oxygen derivatives

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“…This indicates that about 40 indole groups of the tryptophans [35] [calculated in a large (Na+,K+)-ATPase macromolecule] are distributed between internal and surface regions and a part of the chromophores of classes S and I can be in contact with hydrocarbon regions of a lipid membrane. The wide distribution of tryptophan residues throughout the protein volume means that, if a large-scale structural rearrangement does occur upon a change of the enzyme functional state, it is highly probably that this rearrangement would involve the regions of localization of at least some tryptophan residues.…”

Section: State Of Tryptoplzan Residues As Revealed By Intrinsic Fluormentioning

confidence: 99%

Lack of Gross Protein Structure Changes in the Working Cycle of (Na⁺, K⁺)‐Dependent Adenosinetriphosphatase

Chetverin¹,

Venyaminov²,

Emelyanenko³

et al. 1980

European Journal of Biochemistry

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Infrared and tryptophan fluorescence spectra of practically all sufficiently stable functional con~plexes of a highly purified preparation of membrane-bound (Na', K +)-dependent ATPase have been measured. The formation of any functional complex was not accompanied by any considerable change of either shape or position of the tryptophan fluorescence spectrum. Only in the presence of adenine nucleotides was there a small decrease of fluorescence intensity (by 5 -8 %), which apparently results from a change of the sample light scattering. Analysis of the results obtained leads to the conclusion that the environment of no more than one or a few tryptophan residues may differ in all the (Na', K+)-ATPase complexes studies. A comparison of infrared protein spectra in the region of amide I band showed that at any wavenumber the differences between them did not exceed 3 % of the maximum absorption. This means that no more than 3 % of protein peptide groups can change their conformation upon transition between the enzyme functional states. These results, obtained by two independent techniques, allow us to conclude that even if changes of the internal protein structure occur during the working cycle of this transport system, they have an extremely local character.

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Acetyl nitrite: a useful nitrosating reagent

Abstract: Acetyl nitrite has been prepared, and shown to be a useful reagent for the study of the mechanism of deamination of primary amines.

Cited by 12 publications

References 1 publication

GAP1, the general amino acid permease gene of Saccharomyces cerevisiae

GAP1, the general amino acid permease gene of Saccharomyces cerevisiae

cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils

Lack of Gross Protein Structure Changes in the Working Cycle of (Na⁺, K⁺)‐Dependent Adenosinetriphosphatase

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Acetyl nitrite: a useful nitrosating reagent

Abstract: Acetyl nitrite has been prepared, and shown to be a useful reagent for the study of the mechanism of deamination of primary amines.

Cited by 12 publications

References 1 publication

GAP1, the general amino acid permease gene of Saccharomyces cerevisiae

GAP1, the general amino acid permease gene of Saccharomyces cerevisiae

cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils

Lack of Gross Protein Structure Changes in the Working Cycle of (Na+, K+)‐Dependent Adenosinetriphosphatase

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Lack of Gross Protein Structure Changes in the Working Cycle of (Na⁺, K⁺)‐Dependent Adenosinetriphosphatase