Two identical hydrophobic clusters are present on the same actin monomer: interaction between one myosin subfragment-1 and two actin monomers.
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 (A1 and A2) 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 A1 and A2 take place through myosin subfragment-1 (63 kDa-31 kDa) connecting segment.
Labbé
J P
JP
UPR 9008 Centre de Recherches de Biochimie Macrmoléculaire (CNRS), U249 (INSERM), Montpellier, France.
Boyer
M
M
Benyamin
Y
Y
D000199:Actins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009119:Muscle Contraction; D018482:Muscle, Skeletal / Q000737:chemistry; D015879:Myosin Subfragments / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011817:Rabbits
D000199:Actins; D015879:Myosin Subfragments