Abstract
When exposed to various stresses including heat shock, myxoamoebae, growing haploid cells of Physarum polycephalum, show marked morphological changes and consequently become disk-shaped microcysts. We have found that p66 is induced exclusively in the course of microcyst formation and has an actin-binding activity. In this study, we purified p66 to homogeneity and isolated a p66 cDNA. The deduced protein sequence contained 601 amino acids and showed 31% identity to a yeast actin-interacting protein, AIP1. Northern blot analysis revealed that the amount of p66 mRNA was significantly increased by heat shock in myxoamoebae but not in plasmodia. Thus, p66 seems to be a developmentally-expressed stress protein which regulates the rearrangement of actin organization during microcyst formation in P. polycephalum.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism
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Amino Acid Sequence
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Animals
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Base Sequence
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Cloning, Molecular
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DNA, Complementary / analysis
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Fungal Proteins / chemistry
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Fungal Proteins / genetics*
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Fungal Proteins / metabolism
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Heat-Shock Proteins / genetics*
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Heat-Shock Proteins / isolation & purification
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Heat-Shock Proteins / physiology
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Hot Temperature
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics*
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Microfilament Proteins / metabolism
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Molecular Sequence Data
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Physarum polycephalum / genetics*
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Physarum polycephalum / metabolism
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RNA, Messenger / biosynthesis
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Saccharomyces cerevisiae / metabolism
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Sequence Homology, Amino Acid
Substances
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Actins
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DNA, Complementary
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Fungal Proteins
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Heat-Shock Proteins
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Microfilament Proteins
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RNA, Messenger
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actin interacting protein 1
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stress protein, 66-kDa (Physarum)