Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1

Schröder, Rasmus R.; Manstein, Dietmar J.; Jahn, Werner; Holden, Hazel M.; Rayment, Ivan; Holmes, Kenneth C.; Spudich, James A.

doi:10.1038/364171a0

Cited by 290 publications

(233 citation statements)

References 18 publications

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“…On the other hand, cortactin-B and -C showed no effect on the viscosity of F-actin. Consistent with this, the binding of 125 I-labelled F-actin to cortactin-A was inhibited by an excess of myosin subfragment 1 (S1), a well characterized protein which binds along the sides of F-actin (Rayment et al 1993;Schröder et al 1993) (Fig. 2D).…”

Section: The F-actin-binding Properties Of Cortactin-a -B and -Csupporting

confidence: 62%

Isolation and characterization of cortactin isoforms and a novel cortactin‐binding protein, CBP90

Ohoka¹,

Takai

1998

Genes to Cells

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Section: The F-actin-binding Properties Of Cortactin-a -B and -Csupporting

confidence: 62%

Isolation and characterization of cortactin isoforms and a novel cortactin‐binding protein, CBP90

Ohoka¹,

Takai

1998

Genes to Cells

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“…Hydrophobic residues of motif A2 were included in the interface of one actin monomer with S1 and motif A1 was described as being included in the interface of S1 with a second monomer as seen in 3D atomic model of actin-S1 [4].…”

Section: Precise Local Analysis Of Hydrophobic Motifs 4 and B Inmentioning

confidence: 99%

“…Number and vertical lines correspond to amino-acid positions. The sequences corresponding to the t!~ree actin contacts [4] are specified by 1, 2, 3, with a first actin monomer and the fourth contact with a second actin monomer.…”

Section: Precise Local Analysis Of Hydrophobic Motifs 4 and B Inmentioning

confidence: 99%

“…The HCA plot of scallop or rabbit myosin S1 sequences ~ 560-580) revealed the presence of the particulary loop at the +unction N-terminal 63 kDa and the C-terminal 31 kDa [4]. ~_ctin residues 144, 341,345, 349 and 352 (motif A2) located on me monomer were shown by EM and image analysis [3] to be ~n contact with residues 529, 530, 535, 541 and 542 (contact 2) ocated in the N-terminal 63-kDa fragment of S1 (Fig.…”

Section: Precise Local Analysis Of Hydrophobic Motifs 4 and B Inmentioning

confidence: 99%

“…Atomic resolution of the actin structure [1,2] and the threeciimensional atomic model of F-actin decorated with rabbit ~aymotryptic-S1 [3] or Dictyostelium myosin S1 [4] revealed I ~cations of the myosin head on F-actin. This molecular model f the actin-myosin complex derived from the X-ray structure l zveals a close contact between a myosin subfragment-I and 1 ~o actin monomers.…”

Section: ~ Introductionmentioning

confidence: 99%

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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

Labbé¹,

Boyer²,

Benyamin³

1995

FEBS Letters

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Two-dimensional hydrophobic clusters analysis (IICA) 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-I ATP-independent binding sites. HCA suggested the presence of two groups of identical hydrophobic motifs (A~ 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 A~ and A 2 take place through myosin subfragment-I (63 kDa-31 kDa) connecting segment.1~ ey words'," Acto-myosin; Hydrophobic cluster; Structure comparison 1~ IntroductionIdentification of the actin-myosin interface is essential in t nderstanding the cyclical enzymatic and mechanical process c f myofibrillar contraction.Atomic resolution of the actin structure [1,2] and the threeciimensional atomic model of F-actin decorated with rabbit ~aymotryptic-S1 [3] or Dictyostelium myosin S1 [4] revealed I ~cations of the myosin head on F-actin. This molecular model f the actin-myosin complex derived from the X-ray structure l zveals a close contact between a myosin subfragment-I and 1 ~o actin monomers. A first contact includes carboxyl residues ,2, 3, 4, 24, 25, 99 and 100. In a second contact, exposed actin 1 ydrophobic residues 144, 341,345,349 and 352 are concerned. "he third contact involves proline residues (332-333) of actin. ~11 of these contacts involve a single monomer. A second mon-~,mer is close to the myosin heavy chain and the interaction i ~cludes the cz-helix formed by actin residues Trp79 to Asn92 flat formed a weak binding contact and was cross-linked [5,6].The Taylor-Amos model [7] of acto-S1 suggests that S1 has n extensive contact with an actin monomer (acl) and a weaker ,. ontact with an adjacent actin monomer (ac2); and two differ-,, nt rigor complexes were suggested [8,9], with SI binding to :-actin occurring in two steps with actin monomers. Using .,uccessively EDC and DMS, we previously cross-linked two lnonomers to 20-kDa and 50-kDa skeletal S1 fragments, re-: Corresponding author. Fax: (33) (67) 60 94 78.spectively [10], and in vitro studies showed that subfragment-I alone can produce the sliding movement of the actin filament [111.Chemical cross-linking [12], NMR [13,14] and immunochemical studies [15,16,[17][18][19][20] have pinpointed actin segments in subdomain-1, residues 1 28, 96-103, 112-125, 338 348 and 360-372 which are able to bind with the myosin head.Furthermore, the (27 kDa-50 kDa-20 kDa) trypsin split myosin subfragment-1, which could no longer be activated by actin, did not bind to the two sites located in the 96-125 region, but it still interacted with the 338-348 and 360--372 segments [191. The presence of hydrophobic interactions in the actin myosin complex have already been sugge...

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Immunolocalization of myosin Iβ in the hair cell's hair bundle

Metcalf

1998

Cell Motil. Cytoskeleton

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The hair bundle, the hair cell's sensory organelle, transduces acoustical or vestibular stimulation into a change in membrane potential. The actin‐based stereociliary processes of the hair bundle contain a number of myosin isoforms that may be important to the bundle's function. One of these isoforms, myosin Iβ, has been proposed to constitute an adaptation motor controling sensitivity of the hair bundle to mechanical displacement. To gain insight into myosin Iβ's function, its distribution within the hair bundle was examined. A polyclonal antibody was produced that recognizes a protein surface loop within the head domain of myosin Iβ. This antibody was used to localize myosin Iβ in the hair cell by indirect‐immunofluorescence microscopy and indirect‐immunoelectron microscopy. Within the hair bundle, myosin Iβ immunoreactivity was located along the sides of the stereociliary actin core, concentrated in the distal two‐thirds of the stereocilia. Within the hair cell soma, myosin Iβ immunoreactivity was located throughout the cytoplasm exclusive of the cuticular plate. Cell Motil. Cytoskeleton 39:159–165, 1998. © 1998 Wiley‐Liss, Inc.

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Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1

Cited by 290 publications

References 18 publications

Isolation and characterization of cortactin isoforms and a novel cortactin‐binding protein, CBP90

Isolation and characterization of cortactin isoforms and a novel cortactin‐binding protein, CBP90

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

Immunolocalization of myosin Iβ in the hair cell's hair bundle

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