Neurospora crassa mitochondria contain two forms of a 4'-phosphopantetheine-modified protein

When Neurospora crassa was labeled with [14C]pantothenic acid during growth, the mitochondrial fraction contained two bands of radioactivity of Mr 19,000 and 22,000 by sodium dodecyl sulfate gel electrophoresis. The 19-kDa band was converted to the 22-kDa band by four treatments which are characteri...

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Bibliographic Details
Published in:The Journal of biological chemistry 1986-04, Vol.261 (11), p.4785-4788
Main Authors: Lakin-Thomas, P L, Brody, S
Format: Article
Language:English
Subjects:
Acyl Carrier Protein - metabolism
Analytical, structural and metabolic biochemistry
Binding and carrier proteins
Biological and medical sciences
Cell Membrane - metabolism
Dithiothreitol - pharmacology
Electrophoresis, Polyacrylamide Gel
Escherichia coli - analysis
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
Hydrogen-Ion Concentration
Hydroxylamine
Hydroxylamines - pharmacology
Isoelectric Point
Mercaptoethanol - pharmacology
Mitochondria - metabolism
Molecular Weight
Neurospora - ultrastructure
Neurospora crassa - ultrastructure
Pantetheine - analogs & derivatives
Pantetheine - metabolism
Proteins
Sulfhydryl Compounds - metabolism
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Summary:When Neurospora crassa was labeled with [14C]pantothenic acid during growth, the mitochondrial fraction contained two bands of radioactivity of Mr 19,000 and 22,000 by sodium dodecyl sulfate gel electrophoresis. The 19-kDa band was converted to the 22-kDa band by four treatments which are characteristic of the cleavage of a thioester bond: dithiothreitol and 2-mercaptoethanol at basic but not neutral pH, alkaline methanolysis, sodium borohydride in tetrahydrofuran, and hydroxylamine at neutral pH. Mitochondrial subfractionation indicated that the 22-kDa form was preferentially associated with the soluble fraction while the 19-kDa form was found in all fractions. Several properties of the mitochondrial protein were similar to the Escherichia coli acyl carrier protein: Mr on sodium dodecyl sulfate gels, decreased electrophoretic mobility under deacylating conditions, isoelectric point, and covalent attachment of 4'-phosphopantetheine. The 19- and 22-kDa bands may therefore represent acylated and deacylated forms of a mitochondrial acyl carrier protein.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)89173-1