Effects of pressure on actomyosin systems

Ikkai, Takamitsu; Ooi, Tatsuo

doi:10.1021/bi00834a054

Cited by 50 publications

(25 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since previous work has suggested that pressure treatment depolymerizes these proteins (Ikkai and Ooi 1969;O'Shea et al 1976) our present findings are in keeping with those of Marchalonis (1969).…”

Section: Discussionsupporting

confidence: 91%

“…Actomyosin undergoes changes that can be accounted for in terms of depolymerization to actomyosin monomers (Ikkai and Ooi 1969) and F-actin is believed to be depolymerized into G-actin monomers (Ikkai and Ooi 1966). Since pressures up to 3000 atm (304 MNm-Z) favour the formation of hydrogen bonds and the disruption of hydrophobic bonds (Suzuki et al 1968), it was of interest to characterize the changes taking place on the surface of the proteins using a specific probe for a particular hydrophobic group.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Pressure-Induced Changes in Myofibrillar Proteins

Shea¹,

Tume²

1979

Aust. Jnl. Of Bio. Sci.

View full text Add to dashboard Cite

Natural actomyosin, synthetic actomyosin, myosin and F-actinwere subjected to lactoperoxidasecatalysed iodination with 125 1 before and after exposure to a pressure of 150 MNm-2 • After iodination myosin was split into its subfragments, light and heavy meromyosin, and the actomyosins were separated into their component proteins.The effect of the pressure treatment on the extent of iodine incorporation into both the light and heavy chains of myosin and into actin depended on whether the myosin and actin were present as components of natural or synthetic actomyosin or in the purified state. The results suggest that conformational changes altering the exposure of tyrosine groups are induced in isolated myosin and actin by pressure treatment and are partly prevented when these proteins are combined in synthetic actomyosin and more completely prevented when they are combined in natural actomyosin.

show abstract

Section: Discussionsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Pressure-Induced Changes in Myofibrillar Proteins

Shea¹,

Tume²

1979

Aust. Jnl. Of Bio. Sci.

View full text Add to dashboard Cite

show abstract

“…However, since we took our reading very close to the meniscus and worked at a centrifuge speed of only 30,000 rpm, the pressure head at the point where the actin and HMM separated was only about 6 kg/cm2, only 1% of the pressure necessary for complete inhibition of the actin-HMM ATPase (20). Therefore, it seems only remotely possible that the actin-HMM is being dissociated by pressure.…”

Section: Resultsmentioning

confidence: 99%

Heavy Meromyosin: Evidence for a Refractory State Unable to Bind to Actin in the Presence of ATP

Eisenberg

Dobkin

Kielley

1972

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

View full text Add to dashboard Cite

The binding of actin to heavy meromyosin (HMM) The sliding filament theory of muscle contraction proposes that contraction is caused by the cyclic formation and breakage of links between actin and myosin filaments, accompanied by the hydrolysis of ATP (1). One of the key questions in the biochemistry of muscle is, therefore, the nature of the interaction of actin, myosin, and ATP in vivo. Under in vitro coinditions, at low ionic strength, both F-actin and myosin are filaments and, therefore, the interaction between the two proteins is very difficult to study quantitatively. (9-11). Third, in a kinetic study at 6VC, the data suggested that one H.II\ molecule binds to one actin monomer in contrast to the one-to-two ratio observed in the absence of ATP (12).In the light of these differences in the interaction of actin with HMTM in the presence and absence of ATP, we have investigated this interaction in the presence of ATP using both ATPase (ATP phosphohydrolase EC 3.6.1.3) studies and analytical ultracentrifugation.

show abstract

“…MyHC binding to F-actin functions as a molecular motor by transducing chemical energy from ATP hydrolysis into mechanical work (Spudich, 1994). Because high pressure dissociates the complex between F-actin and HMM (Ikkai and Ooi, 1969), this binding increases the volume. A previous study revealed that actin protein from deep-sea fishes had no substitutions in the contact regions with MyHC relative to non-deep-sea fishes (Morita, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…Myosin functions as an actin-based molecular motor that transduces chemical energy obtained by ATP hydrolysis into mechanical work (Spudich, 1994). Although it is unclear what influence high pressure has on this function, high pressure is known to dissociate the complex between F-actin and heavy meromyosin (HMM) (Ikkai and Ooi, 1969). In a previous study, no amino acid substitutions in the MyHC-binding sites of deep-sea fish actin were found (Morita, 2003).…”

Section: Introductionmentioning

confidence: 99%

Comparative sequence analysis of myosin heavy chain proteins from congeneric shallow- and deep-living rattail fish (genus Coryphaenoides)

Morita

2008

Journal of Experimental Biology

View full text Add to dashboard Cite

SUMMARYThe evolutionary adaptations of functional genes to life at high pressure are not well understood. To elucidate the mechanisms of protein adaptation to high pressure, we cloned the myosin heavy chain (MyHC) cDNA from skeletal muscle of two deep-sea fishes, Coryphaenoides yaquinae and C. armatus, and two non-deep-sea fishes, C. acrolepis and C. cinereus. The MyHCs of deep-sea fishes have a unique structure in two loop regions, loop-1 and loop-2, in comparison with those of non-deep-sea fishes. The loop-1 region of deep-sea fishes has a Pro residue and the loop-2 region, which is an actin-binding site, is shorter than the same region in non-deep-sea fishes. The amino acid substitution in the loop-1 region is expected to be mainly involved in ATPase activity, whereas the deletion in the loop-2 region affects the association of MyHC with actin filaments at high pressure. In addition, the MyHC of deep-sea fishes has biased amino acid substitutions at core positions in the coiled-coil structure of the rod region. These amino acid substitutions are likely to decrease the cavities in the coiled-coil structure and consequently make the structure more compact and unaffected by high pressure. Together, these results indicate that amino acid substitutions can adaptively alter the pressure sensitivity of a protein even if they do not directly influence core structure.

show abstract

Effects of pressure on actomyosin systems

Cited by 50 publications

References 17 publications

Pressure-Induced Changes in Myofibrillar Proteins

Pressure-Induced Changes in Myofibrillar Proteins

Heavy Meromyosin: Evidence for a Refractory State Unable to Bind to Actin in the Presence of ATP

Comparative sequence analysis of myosin heavy chain proteins from congeneric shallow- and deep-living rattail fish (genus Coryphaenoides)

Contact Info

Product

Resources

About