Isolation, purification and characterization of myosin B from myxomycete plasmodium

Hatano, Sadashi; Tazawa, Masashi

doi:10.1016/0005-2795(68)90011-1

Cited by 135 publications

(54 citation statements)

References 30 publications

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“…The absence of phosphocreatine and phosphoarginine in Physarurn plasmodia confirms previous reports [3,5]. Absence of AMP suggests that myokinase activity, which is present in natural actomyosin preparations [7,23], may be low in the living plasmodia and that ATP pyrophosphohydrolase, whose activity is very high in the extract of plasmodial cells [24], may exist in an inactive form in the living plasmodia.…”

Section: Discussionsupporting

confidence: 86%

³¹P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

1984

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31P-nuclear magnetic resonance spectra were obtained from intact plasmodial cells of Physarum polycephalum, where cytoplasmic streaming is generated by actin-myosin-ATP interaction. Several peaks were resolved and identified. They included ATP, ADP, orthophosphate and polyphosphates. Peaks for phosphocreatine, phosphoarginine or AMP were not detected. The intracellular pH and concentrations of ATP and free Mgz+ were estimated to be pH 6.9,0.2-0.5 mM, and about 1 mM, respectively. "P-NMR Intracelhdar pH ATP Mg=+Physarum polycephalum Actomyosin

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Section: Discussionsupporting

confidence: 86%

³¹P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

1984

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“…1B). The cortical acto-myosin network consists of actin filaments, myosin filaments and additional cross-linking proteins (Adelman and Taylor, 1969;Hatano and Oosawa, 1966;Hatano and Tazawa, 1968;Pollard, 1981). The actin filaments are arranged isotropically within the cortex (Kane, 1983;Pollard and Korn, 1973;Stossel, 1984), but without any particular orientation, and are connected to each other by myosin and other cross-linking proteins.…”

Section: Introductionmentioning

confidence: 99%

Acto-myosin reorganization and PAR polarity inC. elegans

2007

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The symmetry-breaking event during polarization of C. elegans embryos is an asymmetric rearrangement of the acto-myosin network, which dictates cell polarity through the differential recruitment of PAR proteins. The sperm-supplied centrosomes are required to initiate this cortical reorganization. Several questions about this event remain unanswered: how is the actomyosin network regulated during polarization and how does acto-myosin reorganization lead to asymmetric PAR protein distribution? As we discuss, recent studies show that C. elegans embryos use two GTPases, RHO-1 and CDC-42, to regulate these two steps in polarity establishment. Although RHO-1 and CDC-42 control distinct aspects of polarization, they function interdependently to regulate polarity establishment in C. elegans embryos.

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“…Physarum plasmodia show cytoplasmic shuttle streaming based on an actin-associating motile system (12,15). The shuttle streaming, which is caused by a rhythmical contraction-relaxation cycle of cytoplasmic actomyosin biochemically, is associated morphologically with the sol-gel transformation of cytoplasm.…”

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confidence: 99%

Mechanism of regulation of actin polymerization by Physarum profilin.

Ozaki¹,

Hatano²

1984

The Journal of Cell Biology

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Physarum profilin reduces the rates of nucleation and elongation of F-actin and also reduces the extent of polymerization of actin at the steady state in a concentrationdependent fashion . The apparent critical concentration for polymerization of actin is increased by the addition of profilin . These results can be explained by the idea that Physarum profilin forms a 1 :1 complex with G-actin and decreases the concentration of actin available for polymerization . The dissociation constant for binding of profilin to G-actin is estimated from the kinetics of polymerization of G-actin and elongation of F-actin nuclei and from the increase of apparent critical concentration in the presence of profilin . The dissociation constants for binding of Physarum profilin to Physarum and muscle actins under physiological ionic conditions are in the ranges of 1 .4-3 .7 ,.M and 11

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Isolation, purification and characterization of myosin B from myxomycete plasmodium

Cited by 135 publications

References 30 publications

³¹P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

³¹P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

Acto-myosin reorganization and PAR polarity inC. elegans

Mechanism of regulation of actin polymerization by Physarum profilin.

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Isolation, purification and characterization of myosin B from myxomycete plasmodium

Cited by 135 publications

References 30 publications

31P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

31P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

Acto-myosin reorganization and PAR polarity inC. elegans

Mechanism of regulation of actin polymerization by Physarum profilin.

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³¹P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum

³¹P‐nuclear magnetic resonance studies of intact plasmodia of Physarum polycephalum