Arthrin: A new actin-like protein in insect flight muscle

Bullard, Belinda; Bell, J.L; Craig, Roger; Leonard, Kevin

doi:10.1016/0022-2836(85)90203-7

Cited by 51 publications

(25 citation statements)

References 38 publications

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“…28,30 Suspensions of washed myofibrils in an Eppendorf tube were incubated for 2-3 h in blocking buffer with 1% (w/v) BSA and 2% (v/v) goat serum in relaxing solution 2 (0.1 M NaCl, 20 mM sodium phosphate pH 6.8, 5 mM MgCl 2 , 5 mM EGTA, 5 mM ATP, 5 mM NaN 3 ). After blocking, the myofibrils were separated into two tubes: mouse anti-F1 was added to one tube and mouse anti-F2 was added to the other; antibodies were diluted 1:10 in blocking buffer and myofibrils were incubated overnight.…”

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

Regulation of Oscillatory Contraction in Insect Flight Muscle by Troponin

Kržič

Rybin

Leonard

et al. 2010

Journal of Molecular Biology

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Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

Regulation of Oscillatory Contraction in Insect Flight Muscle by Troponin

Kržič

Rybin

Leonard

et al. 2010

Journal of Molecular Biology

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“…However, these preparations contain arthrin, a stable post-translationally ubiquitinated form of ACT88F (15). No differences in polymerization, activation of myosin ATPase, or myosin binding have been found between actin and arthrin from either Lethocerus (39) or Drosophila.…”

Section: Minipreparation Of Actin-mentioning

confidence: 99%

Actin Residue Glu93 Is Identified as an Amino Acid Affecting Myosin Binding

Razzaq

Schmitz

Veigel

et al. 1999

Journal of Biological Chemistry

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Many mutants have been described that affect the function of the actin encoded by the Drosophila melanogaster indirect flight muscle-specific actin gene, Act88F. We describe the development of procedures for purification of this actin from the other isoforms expressed in the fly as well as in vitro motility, single molecule force/ displacement measurements, and stop-flow solution kinetic studies of the wild-type actin and that of the E93K mutation of the Act88F gene. We show that this mutation affects in vitro motility of F-actin, in both the presence and absence of methylcellulose, and the ability of the ACT88F actin to bind the S1 fragment of rabbit skeletal myosin. However, optical tweezer measurements of the actomyosin working stroke and the force transmitted from the rabbit heavy meromyosin to and through Factin are unchanged by the mutation. These results support the proposal (Holmes, K. C. (1995) Biophys J. 68, (suppl.) 2-7) that actin residue Glu 93 is part of the secondary myosin binding site and suggest that myosin binding occurs first at the primary myosin binding site and then at the secondary site.Actin and myosin are ubiquitous in eukaryotic cells, where they form one of the major motor protein systems. The atomic structure determinations of the actin monomer (2) and the S1 fragment (motor domain) of the chicken skeletal muscle myosin (3) were major landmarks in our understanding of how this motor system works.

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“…The suspension (10 µl) was added to B1 (7 µM) in a total volume of 80 µl of binding buffer, and incubated at room temperature for 1 h. Actin was prepared from rabbit back muscle. 46 Actin (4 µM) was added to B1 (7 µM) in 100 µl of binding buffer and incubated at room temperature for 1 h. Samples of thick filaments alone, actin alone and B1 alone were treated similarly. The mixtures were centrifuged in a Beckman Airfuge for 30 min at 28 psi.…”

Section: Protein Binding Assaymentioning

confidence: 99%

Modular Proteins from the Drosophila sallimus (sls) Gene and their Expression in Muscles with Different Extensibility

Burkart

Qiu

Brendel

et al. 2007

Journal of Molecular Biology

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135

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Article:Burkart, C., Qiu, F., Brendel, S. et al. ReuseUnless indicated otherwise, fulltext items are protected by copyright with all rights reserved. The copyright exception in section 29 of the Copyright, Designs and Patents Act 1988 allows the making of a single copy solely for the purpose of non-commercial research or private study within the limits of fair dealing. The publisher or other rights-holder may allow further reproduction and re-use of this version -refer to the White Rose Research Online record for this item. Where records identify the publisher as the copyright holder, users can verify any specific terms of use on the publisher's website. TakedownIf you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing eprints@whiterose.ac.uk including the URL of the record and the reason for the withdrawal request. Please cite this article as: Burkart, C . ,Q i u ,F . ,B r e n d e l ,S . ,B e n e s ,V . ,H aåg, P., Labeit, S., This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. (700) extend from the Z -disc to the ends of the thick filaments, though, Sls(700) is only in the myofibril core. These shorter isoforms would contribute to the high stiffness of IFM. Other muscles in the thorax and legs have longer Sls isoforms with varying amounts of PEVK sequence; all span the I-band to the ends of the thick filaments. In muscles with longer Ibands, the proportion of PEVK sequence would determine the extensibility of the sarcomere. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT

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Arthrin: A new actin-like protein in insect flight muscle

Cited by 51 publications

References 38 publications

Regulation of Oscillatory Contraction in Insect Flight Muscle by Troponin

Regulation of Oscillatory Contraction in Insect Flight Muscle by Troponin

Actin Residue Glu93 Is Identified as an Amino Acid Affecting Myosin Binding

Modular Proteins from the Drosophila sallimus (sls) Gene and their Expression in Muscles with Different Extensibility

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