Multiple Phenylalanyl-Transfer Ribonucleic Acid Synthetase Activities in the Cytoplasm of Neurospora Crassa

Several tRNA's specific for a particular amino acid have been shown to exist in multiple, or isoaccepting, forms. There is considerable interest in establishing whether multiple aminoacyl-tRNA synthetases also exist. We present evidence that the cytoplasm of Neurospora crassa contains three chr...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 62; no. 4; pp. 1137 - 1144
Main Authors Kull, Fredrick J., Jacobson, K. Bruce
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.04.1969
National Acad Sciences
Subjects
Amino acids
Biochemistry
Biological Sciences: Biochemistry
Carbon Isotopes
Chromatography
Cytoplasm
Cytoplasm - enzymology
Enzymes
Ligases
Neurospora
Neurospora crassa
Phenylalanine
Phosphates
Quaternary ammonium compounds
RNA, Transfer
Sulfates
Transfer RNA
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Summary:Several tRNA's specific for a particular amino acid have been shown to exist in multiple, or isoaccepting, forms. There is considerable interest in establishing whether multiple aminoacyl-tRNA synthetases also exist. We present evidence that the cytoplasm of Neurospora crassa contains three chromatographically separable phenylalanyl-tRNA synthetases distinct from mitochondrial phenylalanyl-tRNA synthetase. In addition to differences in chromatographic properties the three enzymes exhibit different affinities, in Tris-Cl buffer, toward purified species of valine and alanine tRNA's isolated from Escherichia coli. The two major chromatographic fractions have very similar sedimentation characteristics, which makes a monomer-dimer relationship unlikely.
Bibliography:ObjectType-Article-1
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This research was sponsored by the U.S. Atomic Energy Commission under contract with the Union Carbide Corporation.
Biology Division postdoctoral investigator.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.62.4.1137