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Two identical hydrophobic clusters are present on the same actin monomer: interaction between one myosin subfragment‐1 and two actin monomers
Author(s) -
Labbé Jean-Pierre,
Boyer Mireille,
Benyamin Yves
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01044-f
Subject(s) - monomer , myosin , actin , chemistry , biophysics , actin binding protein , actin remodeling , myosin head , myosin light chain kinase , polymer , biochemistry , biology , cytoskeleton , actin cytoskeleton , organic chemistry , cell
Two‐dimensional hydrophobic clusters analysis (HCA) was used to compare the distribution of hydrophobic clusters along various actin sequence. HCA‐deduced patterns were not altered by amino‐acid variations throughout the evolution of actin and we observed similar hydrophobic motifs comprising myosin subfragment‐1 ATP‐independent binding sites. HCA suggested the presence of two groups of identical hydrophobic motifs (A 1 and A 2 ) which bound on each side of the S1 (63 kDa‐31 kDa) connecting segment in relation with two actin monomers. This connection is important in communications between actin‐ and nucleotide‐binding sites. We postulate that some relation and message between the two motifs A 1 and A 2 take place through myosin subfragment‐1 (63 kDa‐31 kDa) connecting segment.