Two identical hydrophobic clusters are present on the same actin monomer: interaction between one myosin subfragment‐1 and two actin monomers

FEBS Letters

Benyamin, Yves¹  Labbé, Jean-Pierre¹  Boyer, Mireille¹ 

[1] UPR 9008 Centre de Recherches de Biochimie Macromoléculaire (CNRS), U249 (INSERM), Laboratoire de Recherches sur la Motilité Cellulaire (EPHE), Université Montpellier-1, BP 5051, F-34033 Montpellier Cédex, France

关键词: Acto-myosin;    Hydrophobic cluster;    Structure comparison;   

DOI  :  10.1016/0014-5793(95)01044-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown