Abstract
Limited proteolysis of bacteriophage T7 primase/helicase with endoproteinase Glu-C produces several proteolytic fragments. One of these fragments, which is derived from the C-terminal region of the protein, was prepared and shown to retain helicase activity. This result supports a model in which the gene 4 proteins consist of functionally separable domains. Crystals of this C-terminal fragment of the protein have been obtained that are suitable for X-ray diffraction studies.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallization
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DNA Helicases / chemistry*
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DNA Primase
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Hydrolysis
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Kinetics
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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RNA Nucleotidyltransferases / chemistry*
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Serine Endopeptidases / metabolism
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Thymine Nucleotides / metabolism
Substances
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Peptide Fragments
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Thymine Nucleotides
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DNA Primase
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RNA Nucleotidyltransferases
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Serine Endopeptidases
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glutamyl endopeptidase
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DNA Helicases
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thymidine 5'-triphosphate