Regulatory light chain influences alterations of myosin head induced by actin

Babiychuk, Eduard B.; Stȩpkowski, Dariusz; Danilova, V. M.; Kakol, I

doi:10.1016/0014-5793(91)81383-j

Cited by 8 publications

(3 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, it is reasonable to conclude that the Nterminus of A1 is involved in the process of modulation of myosin head interaction with actin. The present results confirm the previous observation that both light chains of skeletal myosin: regulatory and essential communicate with each other and influence the motor domain of myosin head [10,18,20].…”

Section: Discussionsupporting

confidence: 92%

See 1 more Smart Citation

The shortening of the N‐terminus of myosin essential light chain A1 influences the interaction of heavy meromyosin with actin

et al. 1998

View full text Add to dashboard Cite

The effects resulting from the removal of the N-terminus of heavy meromyosin (HMM) A1 light chain by papain digestion are investigated. The fluorometry of TRITCphalloidin labelled actin in ghost fibers is used as a tool for sensing conformational changes of rigor complex of phosphorylated and dephosphorylated HMM with actin filament. The experiments were performed both under conditions assuring saturation of RLC with magnesium cation (4 mM EGTA) or calcium cation (0.1 mM CaCI2), and in constant presence of 1 mM magnesium chloride. HMM native and with A1 shortened from the N-terminus is used. As it was observed previously rigor complex of actin filament and native HMM shows sensitivity to the kind of cation saturating RLC and to the phosphorylation status of RLC. In particular, the sin20 parameter of actin bound rhodamine-phalloidin fluorescence polarization representing roughly the flexibility of actin filament HMM complex changes significantly with the changes of RLC phosphorylation and cation saturation. Removal of the N-terminus of A1 reduces this sensitivity to cation and phosphorylation both in the case of dephosphorylated and phosphorylated HMM. Our results suggest that the N-terminus of A1 plays significant role in the rigor interaction of myosin heads with actin and is involved in modulatory function of RLC in this interaction.

show abstract

Section: Discussionsupporting

confidence: 92%

“…Rabbit back muscles were extracted and myosin purified in phosphorylated and dephosphorylated form as described previously [9,10]. Phosphorylated and dephosphorylated HMM was prepared by brief digestion of soluble phosphorylated and dephosphorylated myosin with chymotrypsin in the presence of CaCI2.…”

Section: Methodsmentioning

confidence: 99%

The shortening of the N‐terminus of myosin essential light chain A1 influences the interaction of heavy meromyosin with actin

et al. 1998

View full text Add to dashboard Cite

show abstract

“…(a) The rate of tryptic digestion of the myosin heavy chain in the 20/50 kDa junction in the presence of actin was dependent both on phosphorylation and the kind of cation saturating the regulatory light chain (Mg 2÷ or Ca 2+) [46].…”

Section: The Role Of Light Chains and Their N-terminal Parts In The Mmentioning

confidence: 99%

The role of the skeletal muscle myosin light chains N‐terminal fragments

Stȩpkowski

1995

FEBS Letters

View full text Add to dashboard Cite

The myosin regulatory and essential fight chains in skeletal muscle do not play a role as significant as in scallop or smooth muscle, however, there are some data suggesting that the skeletal myosin fight chains and their N-terminal parts may have a modulatory function in the interaction of actin with myosin heads. In this paper four conformational states of the myosin head with respect to the regulatory light chain bound cation (magnesium or calcium) and phosphorylation are proposed. Communication between regulatory and essential light chains and putative binding of the N-terminus of A1 essential light chain to actin is discussed.

show abstract