Effect of mild heat treatment on the ATPase activity and proteolytic sensitivity of myosin subfragment-1

Setton, Adrianne; Mühlrád, András

doi:10.1016/0003-9861(84)90214-5

Cited by 48 publications

(39 citation statements)

References 15 publications

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“…0006-2960/87/0426-1492$01.50/0 thermal denaturation at 35 OC (Setton & Muhlrad, 1984). This observation would lend strong credence to the domain hypothesis since it demonstrates that a segment of the S1 (50 kDa) is capable of independent unfolding.…”

mentioning

confidence: 62%

Substructure of skeletal myosin subfragment 1 revealed by thermal denaturation

Burke¹,

Zaager²,

Bliss³

1987

Biochemistry

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The stability of myosin subfragment 1 (S1) to thermal denaturation has been followed by limited tryptic proteolysis. Digestions done during the thermal denaturation show that at temperatures at and above 37 degrees C there is a marked increase in the susceptibility of S1 to tryptic degradation, as evidenced by the loss of all bands corresponding to the normally trypsin-resistant fragments of 50, 27, and 21 kDa of the heavy chain and to the light chain. The enhanced digestion of S1 appears to be due to a general unfolding of all segments of S1, although the 50-kDa segment appears to unfold at a lower temperature than the remainder of the S1 structure. Digestions done after 30-min exposure to higher temperatures or after subsequent cooling to 25 degrees C show marked differences in the susceptibility of the S1 to trypsin. This suggests that, on cooling, a substantial portion of the S1, but not the 50-kDa segment, is capable of refolding to a state corresponding closely to that in the native S1. These data indicate that in terms of thermal denaturation the S1 behaves as though it is comprised of two domains--an unstable 50-kDa domain and a more stable domain comprised of the 27- and 21-kDa segments of the heavy chain interacting with the light chain, as proposed recently by Setton and Muhlrad [Setton, A., & Muhlrad, A. (1984) Arch. Biochem. Biophys. 235, 411-417]. The rates of thermal inactivation of the ATPase of S1 are found to correspond closely to the decay rates for the 50-kDa fragment, suggesting that this segment in S1 is closely associated with the ATPase function of the protein.

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mentioning

confidence: 62%

Substructure of skeletal myosin subfragment 1 revealed by thermal denaturation

Burke¹,

Zaager²,

Bliss³

1987

Biochemistry

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“…Nevertheless, when this central fragment is subjected to thermal denaturation (Setton & Muhlrad, 1984;Burke et al, 1987), an organic solvent , or specific chemical modification (Chaussepied et al, 1986a-f), it has a rather high susceptibility to proteolytic cleavage in comparison with the other fragments of the S-1 heavy chain. This particular instability is significantly stabilized by the presence of Mg-nucleotides (Pinter et al, 1986); the protease sensitivity of this region has also been described for chicken gizzard smooth muscle myosin S-1, which shows the same lability in the absence of denaturing conditions (Bonet et al, 1987).…”

Section: The 50k Sequencementioning

confidence: 99%

Pathway for the communication between the ATPase and actin sites in myosin

Audemard

Bertrand

Bonet

et al. 1988

J Muscle Res Cell Motil

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“…§1734 solely to indicate this fact. the high-temperature regime illustrates "substrate protection" (21,22). Signal loss in this regime can be time dependent.…”

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confidence: 99%

A search for protein structural changes accompanying the contractile interaction.

Johnson

Bivin

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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It appears that small movements (d d hitherto only by fluorescence resonance energy trer measurements and crosulinking studies) in a region of the myosin S-1 particle may mediate chemomechanical energy transduction In the contractile system. Here we find under conditions of hih precision at 10"C and 20°C that ATP binding to S-1 causes small (0.4%) changes In CD signal, Ae2m, as do temperature changes In the regime below 16°C. ATP binding perturbs

show abstract

Effect of mild heat treatment on the ATPase activity and proteolytic sensitivity of myosin subfragment-1

Cited by 48 publications

References 15 publications

Substructure of skeletal myosin subfragment 1 revealed by thermal denaturation

Substructure of skeletal myosin subfragment 1 revealed by thermal denaturation

Pathway for the communication between the ATPase and actin sites in myosin

A search for protein structural changes accompanying the contractile interaction.

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