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Biochemistry (Moscow)

, Volume 82, Issue 2, pp 213–223 | Cite as

Intermolecular interactions of myosin subfragment 1 induced by the N-terminal extension of essential light chain 1

  • D. S. Logvinova
  • O. P. Nikolaeva
  • D. I. LevitskyEmail author
Article

Abstract

We applied dynamic light scattering (DLS) to compare aggregation properties of two isoforms of myosin subfragment 1 (S1) containing different “essential” (or “alkali”) light chains, A1 or A2, which differ by the presence of an N-terminal extension in A1. Upon mild heating (up to 40°C), which was not accompanied by thermal denaturation of the protein, we observed a significant growth in the hydrodynamic radius of the particles for S1(A1), from ~18 to ~600-700 nm, whereas the radius of S1(A2) remained unchanged and equal to ~18 nm. Similar difference between S1(A1) and S1(A2) was observed in the presence of ADP. In contrast, no differences were observed by DLS between these two S1 isoforms in their complexes S1-ADP-BeFx and S1-ADP-AlF 4 which mimic the S1 ATPase intermediate states S1*-ATP and S1**-ADP-Pi. We propose that during the ATPase cycle the A1 N-terminal extension can interact with the motor domain of the same S1 molecule, and this can explain why S1(A1) and S1(A2) in S1-ADP-BeFx and S1-ADP-AlF 4 complexes do not differ in their aggregation properties. In the absence of nucleotides (or in the presence of ADP), the A1 N-terminal extension can interact with actin, thus forming an additional actin-binding site on the myosin head. However, in the absence of actin, this extension seems to be unable to undergo intramolecular interaction, but it probably can interact with the motor domain of another S1 molecule. These intermolecular interactions of the A1 N-terminus can explain unusual aggregation properties of S1(A1).

Keywords

myosin subfragment 1 essential light chains thermally induced aggregation dynamic light scattering 

Abbreviations

A1 and A2

essential (alkali) myosin light chains 1 and 2

AlF4

aluminum fluoride

BeFx

beryllium fluoride

DLS

dynamic light scattering

DSC

differential scanning calorimetry

ELC

essential myosin light chains

S1

myosin subfragment 1

S1(A1) and S1(A2)

S1 isoforms containing different alkali light chains-A1 or A2

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Copyright information

© Pleiades Publishing, Ltd. 2017

Authors and Affiliations

  • D. S. Logvinova
    • 1
    • 2
  • O. P. Nikolaeva
    • 3
  • D. I. Levitsky
    • 1
    • 3
    Email author
  1. 1.Bach Institute of Biochemistry, Research Center of BiotechnologyRussian Academy of SciencesMoscowRussia
  2. 2.Department of Biochemistry, School of BiologyLomonosov Moscow State UniversityMoscowRussia
  3. 3.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

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