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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Labbé JP,Boyer M,Benyamin Y

doi

10.1016/0014-5793(95)01044-f

subject

Has Abstract

pub_date

1995-10-16 00:00:00

pages

221-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01044-F

journal_volume

373

pub_type

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