Role of the myosin light chains in binding to actin

Winstanley, Monica A.; Trayer, Hylary R.; Trayer, Ian P.

doi:10.1016/0014-5793(77)80242-1

Cited by 40 publications

(23 citation statements)

References 13 publications

(17 reference statements)

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“…The A1/A1 homodimers exhibit a stronger affinity than the A2/A2 species for both the monomeric (G) and polymeric (F) forms of actin. This finding is consistent with data on the binding of the S1 species [11], and might be predicted from kinetic parameters obtained for the single head, S-1 fragments [5].…”

supporting

confidence: 92%

“…The glutaraldehyde cross-linked F-actin-tropomyosin complex was prepared and linked to CNBr-activated Sepharose-4B as reported earlier [11]. The N 6 -(6-aminohexyl)-ADP (N 6-ADP) ligand, and the pyrophosphate derivative (6-aminohexan-l-ol pyrophosphate: HAPP) were prepared and attached to Sepharose-4B by the method of Trayer et al [15].…”

Section: Preparation and Operation Of The Affinity Columnsmentioning

confidence: 99%

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The separation of heavy meromyosin isoenzymes by differential actin binding

1977

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supporting

confidence: 92%

Section: Preparation and Operation Of The Affinity Columnsmentioning

confidence: 99%

The separation of heavy meromyosin isoenzymes by differential actin binding

1977

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“…Earlier studies showed that fast skeletal myosin S1 containing MLC1 (long ELC) had a lower apparent K m (higher affinity) for actin and a slower turnover rate of MgATP than myosin S1 containing MLC3 (short ELC) (45,106,108), suggesting that intermolecular contacts between the NH 2 -terminus of MLC1 and actin resulted in a stronger and slower interaction of myosin cross-bridges with actin. These results were supported by affinity chromatography studies (110) and by cosedimentation studies (101) showing that myosin S1 with MLC1 does indeed have a higher affinity for actin than myosin S1 with MLC3. Even though both cardiac ELC isoforms (ELC a and ELC v ) are expressed with their long NH 2 -termini ( Fig.…”

Section: Elc-mediated Regulation Of Actin-myosin Interactionsmentioning

confidence: 70%

“…2). This region was found to play a role in the interaction of the ELC with actin (91,101,110). The COOH-terminal region of ELC (long and short isoforms) was found to interact with the MHC and possibly with the RLC (33,76,112).…”

Section: Structural Features Of Elcmentioning

confidence: 97%

Myosin essential light chain in health and disease

Hernandez¹,

Jones²,

Guzman³

et al. 2007

American Journal of Physiology-Heart and Circulatory Physiology

115

114

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The essential light chain of myosin (ELC) is known to be important for structural stability of the ␣-helical lever arm domain of the myosin head, but its function in striated muscle contraction is poorly understood. Two ELC isoforms are expressed in fast skeletal muscle, a long isoform and its NH 2-terminal ϳ40 amino acid shorter counterpart, whereas only the long ELC is observed in the heart. Biochemical and structural studies revealed that the NH 2-terminus of the long ELC can make direct contacts with actin, but the effects of the ELC on the affinity of myosin for actin, ATPase, force, and the kinetics of force generating myosin cross-bridges are inconclusive. Myosin containing the long ELC has been shown to have slower cross-bridge kinetics than myosin with the short isoform. A difference was also reported among myosins with long isoforms. Increased shortening velocity was observed in atrial compared with ventricular muscle fibers. The common findings suggest that ELC provides the fine tuning of the myosin motor function, which is regulated in an isoform and tissue-dependent manner. The functional importance of the ELC is further implicated by the discovery of ELC mutations associated with Familial Hypertrophic Cardiomyopathy. The pathological phenotypes vary in severity, but more notably, almost all ELC mutations result in sudden cardiac death at a young age. This review summarizes the functional roles of striated muscle ELC in normal healthy muscle and in disease. Transgenic animal models and phenotypic characterization of ELC-mediated remodeling of the heart are also discussed.cross-bridge kinetics; striated muscle contraction; familial hypertrophic cardiomyopathy; sarcomeric mutations; failing heart; sudden cardiac death STRIATED MUSCLE MYOSIN

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“…Hybridization experiments have attributed these kinetic differences unambiguously to the nature of the particular alkali light chain and not to the heavy-chain component [3]. Differences in actin-binding properties are also demonstrated in [4]. b) 5,5'-Dithiobis(2-nitrobenzoic acid) light chain Nbszlight chain, formerly called DTNB-LC and sometimes referred to as LC-2) is phosphorylable, like its homologous P-light chain, in smooth muscle myosin.…”

Section: Edta and Ca2mentioning

confidence: 99%

‘Artificial’ Myosin Isozymes; Preparation and Characteristics

Cardinaud

1982

European Journal of Biochemistry

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Using precisely monitored proteolytic digestion conditions rabbit fast skeletal muscle myosin could be selectively modified in different ways. A myosin isozyme with a 20-kDa alkali light chain 1 (Al) could be obtained by digesting with papain in the presence of Ca2+. Under these conditions alkali light chain 2 (A2) was cleaved at Lys-17 and lost a 2.3-kDa N-terminal fragment including the strongly basic N terminus and about half of the characteristic (Ala-Pro) sequence. The Nbs2-[5,5' dithiobis(2-nitrobenzoic acid)-]light chain and A2 were left unmodified and less than 5% of the myosin heavy chain presented a break in the subfragment-2 region. EDTA and Ca2+ ATPase activities were unchanged. A myosin isozyme with an 18-kDa Nbsz-light chain was obtained by limited digestion with trypsin in the presence of Ca2+. The 18.9-+ 18-kDa conversion was nearly 100% whereas less than 10% of the heavy chain was fragmented and only about 5% of A1 was converted to Al'. The Nbsl-light chain was cleaved at Arg-7 preserving Ser-15 and consequently a phosphorylated modified myosin could be obtained. A quasi-elastic lightscattering study showed that this modified myosin in high-ionic-strength solutions exhibited physicochemical characteristics quite similar to those of unmodified myosin.

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Role of the myosin light chains in binding to actin

Cited by 40 publications

References 13 publications

The separation of heavy meromyosin isoenzymes by differential actin binding

The separation of heavy meromyosin isoenzymes by differential actin binding

Myosin essential light chain in health and disease

‘Artificial’ Myosin Isozymes; Preparation and Characteristics

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