Primary sequence of the alpha-toxin gene from Staphylococcus aureus wood 46
Infection and ImmunityPublished 1 November 1984Open access
G S Gray, Michael Kehoe
Citations168
SJR quartileQ1
SJR score1.05
SNIP0.81
Generate an AI Snapshot to get a quick, structured summary of this paper.
Study Snapshot
ObjectiveStudy objective
MethodsResearch methodology
PopulationPopulation studied
Sample sizeSample sizes
OutcomesStudy outcomes here
ResultsStudy results comes here
LimitationsResearch study limitations comes here
A concise AI-generated summary of the paper will appear here once you click Generate AI Snapshot.
TL;DR
The complete DNA sequence of a cloned alpha-toxin gene from Staphylococcus aureus was determined and the amino acid sequence of the alpha-Toxin protein, predicted from the DNA sequence, was described and compared with published data.
Abstract
The complete DNA sequence of a cloned alpha-toxin gene from Staphylococcus aureus was determined. The amino acid sequence of the alpha-toxin protein, predicted from the DNA sequence, was described and compared with published data. The primary product of the cloned alpha-toxin gene contained a 26-amino-acid leader sequence which possessed characteristic features of a signal sequence involved in secretion. The mature alpha-toxin protein had a molecular size of 33,000 and contained only three short regions of high hydrophobicity in addition to a number of short, weakly hydrophobic regions.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
Journal of Molecular BiologyA simple method for displaying the hydropathic character of a protein
23,075 Citations1982Jack Kyte, Russell F. Doolittle
A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.
Methods in enzymology on CD-ROM/Methods in enzymology[57] Sequencing end-labeled DNA with base-specific chemical cleavages
14,691 Citations1980Allan M. Maxam, Walter Gilbert
Annual Review of BiochemistryEmpirical Predictions of Protein Conformation
3,139 Citations1978Peter Y. Chou, Gerald D. Fasman
Nucleic Acids ResearchCompilation and analysis of<i>Escherichia coli</i>promoter DNA sequences
2,223 Citations1983Diane K. Hawley, William R. McClure
A consensus promoter sequence based on homologies among 112 well-defined promoters was determined that was in substantial agreement with previous compilations.
Annual Review of MicrobiologyTranslational Initiation in Prokaryotes
780 Citations1981Larry Gold, David Pribnow +4 more
A conceptual framework for developing a theory of translational initiation and three approaches to a higher order approximation are described.
The Journal of Cell BiologyOn the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
368 Citations1981R. Füssle, Sucharit Bhakdi +4 more
The possibility is raised that native alpha-toxin oligomerizes on and in the membrane to form an amphiphilic annular complex that, through its partial embedment within the lipid bilayer, generates a discrete transmembrane channel.
Proceedings of the National Academy of SciencesRole of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane.
237 Citations1982S Inouye, Xavier Soberón +4 more
Results indicate that the positively charged amino-terminal region of the signal peptide plays an important role in efficient protein secretion across the membrane.
Pharmacology & TherapeuticsToxins of staphylococcus aureus
160 Citations1982John H. Freer, J ARBUTHNOTI
Journal of BacteriologyInteraction of Staphylococcal α-Toxin with Artificial and Natural Membranes
150 Citations1968John H. Freer, J. P. Arbuthnott +1 more
BiochemistryStudies on the binding of staphylococcal 125I-labeled α-toxin to rabbit erythrocytes
95 Citations1976Paul Cassidy, Sidney Harshman
Simultaneous assays of 125I-labeled alpha-toxin binding and leakage of intracellular 86Rb+ suggest that toxin binding and membrane damage are separate, sequential functions.
Infection and ImmunityExpression of a cloned Staphylococcus aureus alpha-hemolysin determinant in Bacillus subtilis and Staphylococcus aureus
93 Citations1983Neil Fairweather, Sheila Kennedy +3 more
A DNA sequence encoding Staphylococcus aureus alpha-hemolysin, which had been previously cloned and mapped in Escherichia coli K-12, was introduced into Bacillus subtilis BD170 and several strains of S. aUREus by using plasmid vectors, some of which could replicate in all three organisms.
The Journal of Cell BiologyMolecular components of the signal sequence that function in the initiation of protein export.
61 Citations1982Scott D. Emr, Thomas J. Silhavy
The results suggest that a critical subset of four amino acids is contained within the central hydrophobic core of the LamB signal sequence, which may comprise a recognition site that interacts with a component of the cellular export machinery.
Infection and ImmunityCloning, expression, and mapping of the Staphylococcus aureus alpha-hemolysin determinant in Escherichia coli K-12
49 Citations1983Michael Kehoe, James B. Duncan +3 more
A fragment of Staphylococcus aureus DNA encoding the alpha-hemolysin determinant was cloned from strain Wood 46 by inserting Sau3A-generated genomic DNA fragments between the BamHI sites of the lambda replacement vector L47.
BiochemistryPurification and properties of two forms of staphylococcal α-toxin
35 Citations1973Howard R. Six, Sidney Harshman
Journal of BacteriologyTransport and processing of staphylococcal alpha-toxin
23 Citations1983Rodney K. Tweten, K. K. Christianson +1 more
Two larger precursors to staphylococcal alpha-toxin were identified and partially characterized and the peptide maps of the 35S-labeled peptides from extracellular alpha-Toxin and the two precursor were almost identical.
ToxiconChemical studies on staphylococcal alpha-toxin and its fragments
19 Citations1980Iwao Kato, Masashi Watanabe
The present effort was undertaken to identify the Nand C-terminal amino acids of alpha-toxin and to correlate the results with the fragment chain structure of the toxin molecule.
Biochemical and Biophysical Research CommunicationsPhotolabeling of staphylococcal α-toxin from within rabbit erythrocyte membranes
18 Citations1983Monica Thelestam, Colette Jolivet‐Reynaud +1 more
Intrinsic membrane proteins of rabbit red blood cells were labeled with the photoreactive amphipatic reagent 12-(4-azido-2-nitrophenoxy) stearoyl (1-14C) glucosamine, which inserts into the hydrophobic membrane region and generates a reactive nitrene upon ultraviolet irradiation.
Photoactivated Hydrophobic Reagents for Integral Membrane Proteins
12 Citations1982Hagan Bayley
Photoactivated hydrophobic reagents are being developed to label those regions of integral membrane proteins that lie within the hydrocarbon core of the lipid bilayer.