Abstract
We have investigated the physiological function of type 2 methionine aminopeptidases (MetAP2) using Caenorhabditis elegans as a model system. A homolog of human MetAP2 was found in the C. elegans genome, which we termed MAP-2. MAP-2 protein displayed methionine aminopeptidase activity and was sensitive to inhibition by fumagillin. Downregulation of map-2 expression by RNAi led to sterility, resulting from a defect in germ cell proliferation. These observations suggest that MAP-2 is essential for germ cell development in C. elegans and that this ubiquitous enzyme may play important roles in a tissue specific manner.
Copyright 2004 Federation of European Biochemical Societies
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Aminopeptidases / chemistry
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Aminopeptidases / drug effects
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Aminopeptidases / genetics
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Aminopeptidases / metabolism*
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Animals
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Binding Sites
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Caenorhabditis elegans / embryology
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Caenorhabditis elegans / genetics*
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Caenorhabditis elegans Proteins / chemistry
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Caenorhabditis elegans Proteins / drug effects
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Caenorhabditis elegans Proteins / genetics
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Caenorhabditis elegans Proteins / metabolism*
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Cell Division*
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Conserved Sequence
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Cyclohexanes
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Down-Regulation
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Fatty Acids, Unsaturated / pharmacology
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Gene Expression Regulation
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Germ Cells / physiology*
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Larva
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Metalloendopeptidases / chemistry
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Metalloendopeptidases / drug effects
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism*
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Molecular Sequence Data
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RNA Interference
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Sensitivity and Specificity
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Sequence Homology, Amino Acid
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Sesquiterpenes
Substances
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Caenorhabditis elegans Proteins
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Cyclohexanes
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Fatty Acids, Unsaturated
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Sesquiterpenes
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fumagillin
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Aminopeptidases
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methionine aminopeptidase 2
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Metalloendopeptidases