Myosin Rod-Packing Schemes in Vertebrate Muscle Thick Filaments

Squire, John M.; Cantino, Marie E.; Chew, Michael; Denny, Richard; Harford, Jeffrey J.; Hudson, Liam; Luther, Pradeep K.

doi:10.1006/jsbi.1998.3995

Cited by 32 publications

(23 citation statements)

References 39 publications

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“…1,2 It would seem most likely that the number of cMyBPC molecules would be three, considering that myosin rods are most probably arranged in a three-stranded helix, 33 that six, prob- Figure 2. A, Yeast two-hybrid reporter gene activation by different prey cMyBPC domains paired with bait domain C5.…”

Section: Putative True Interactor Clones Obtained From the Yeast Two-mentioning

confidence: 99%

“…ably paired, titin strands lie along the surface of the myosinbackbone, 33,34 and that the position of domain C10, which binds to both titin and myosin, would be dictated by the register of the first Ig-like domain of the titin superrepeats and the MyBPC binding site on the LMM component of myosin. 7,8 Indeed, many different models of the arrangement of MyBPC in the thick filament have been based on three MyBPC molecules.…”

Section: Circulation Research October 18 2002mentioning

confidence: 99%

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Identification of Novel Interactions Between Domains of Myosin Binding Protein-C That Are Modulated by Hypertrophic Cardiomyopathy Missense Mutations

Moolman‐Smook

Flashman

Lange

et al. 2002

Circulation Research

155

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Abstract-Cardiac myosin binding protein-C (cMyBPC) is a modular protein consisting of 11 domains whose precise function and sarcomeric arrangement are incompletely understood. Identification of hypertrophic cardiomyopathy (HCM)-causing missense mutations in cMyBPC has highlighted the significance of certain domains. Of particular interest is domain C5, an immunoglobulin-like domain with a cardiac-specific insert, which is of unknown function yet is the site of two HCM-causing missense mutations. To identify interactors with this region, a human cardiac cDNA library was screened in a yeast two-hybrid (Y2H) assay using the C5 sequence as bait. Screening Ͼ7ϫ10 6 clones surprisingly revealed that domain C5 preferentially bound to clones encoding C-terminal fragments of cMyBPC; the interacting region was narrowed to domain C8 by deletion mapping. A surface plasmon resonance assay using purified recombinant cMyBPC domains was used to measure the affinity of C5 and C8 in vitro (K a ϭ1ϫ10 5 mol/L Ϫ1 ). This affinity was decreased about 2-fold by the HCM mutation R654H, and by at least 10-fold by the mutation N755K. Further Y2H assays also demonstrated specific binding between domains C7 and C10 of cMyBPC. Based on these novel interactions, and previous biochemical and structural data, we propose that cMyBPC molecules trimerize into a collar around the thick filament, with overlaps of domains C5-C7 of one cMyBPC with C8-C10 of another. We speculate that this interaction may be dynamically formed and released, thereby restricting or favoring cross-bridge formation, respectively. We suggest that the HCM mutations act by altering the cMyBPC collar, indicating its importance in thick filament structure and regulation.

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Section: Putative True Interactor Clones Obtained From the Yeast Two-mentioning

confidence: 99%

Section: Circulation Research October 18 2002mentioning

confidence: 99%

Identification of Novel Interactions Between Domains of Myosin Binding Protein-C That Are Modulated by Hypertrophic Cardiomyopathy Missense Mutations

Moolman‐Smook

Flashman

Lange

et al. 2002

Circulation Research

155

View full text Add to dashboard Cite

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“…Firstly, the geometry of this model needs further verification. The diameter of the myosin thick filament is 13-15 nm [82], resulting in a circumference of approximately 41-47 nm. The trimeric collar model proposes that the length of the ring that wraps around the myosin thick filament is 9 immunoglobulin domains.…”

Section: Models For the Assembly Of Mybp-c Onto The Thick Filamentmentioning

confidence: 99%

Myosin binding protein C: Structural abnormalities in familial hypertrophic cardiomyopathy

et al. 2004

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“…Several other classes of filaments made from long coiled-coil proteins have been characterised in many taxa. Amongst these are myosin II bipolar thick filaments in metazoans (Squire et al, 1998) and slime moulds (Bosgraaf and van Haastert, 2006). The families of 2-5 nm fine filaments (Roberts, 1987) include several largely a-helical proteins, with coiled-coil rod domains of several hundred residues.…”

Section: Introductionmentioning

confidence: 99%

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Walshaw

Gillespie

Kelemen

2010

Journal of Structural Biology

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a b s t r a c tIn recent years, a number of bacterial coiled-coil proteins have been characterised which have roles in cell growth and morphology. Several have been shown to have a cytoskeletal function and some have been proposed to have an IF-like character in particular. We recently demonstrated in Streptomyces coelicolor a cytoskeletal role of Scy, a large protein implicated in filamentous growth, whose sequence is dominated by an unusual coiled-coil repeat. We present a detailed analysis of this 51-residue repeat and conclude that it is likely to form a parallel dimeric non-canonical coiled coil based on hendecads but with regions of local underwinding reflecting highly periodic modifications in the sequence. We also demonstrate that traditional sequence similarity searching is insufficient to identify all but the close orthologues of such repeat-dominated proteins, but that by an analysis of repeat periodicity and composition, remote homologues can be found. One clear candidate, despite a great size discrepancy and unremarkable sequence identity, is the known filament-former FilP in the same species. Both proteins appear distinct from the archetypal bacterial IF-like protein; they therefore may constitute a new class of bacterial filamentous protein. The similar sequence characteristics of both suggest their likely oligomer state and a possible mechanism for higher-order assembly into filaments. Another remote homologue in Actinomyces was highlighted by this method. Further, a known coiled-coil protein, DivIVA, appears to share some of these sequence characteristics.

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Myosin Rod-Packing Schemes in Vertebrate Muscle Thick Filaments

Cited by 32 publications

References 39 publications

Identification of Novel Interactions Between Domains of Myosin Binding Protein-C That Are Modulated by Hypertrophic Cardiomyopathy Missense Mutations

Identification of Novel Interactions Between Domains of Myosin Binding Protein-C That Are Modulated by Hypertrophic Cardiomyopathy Missense Mutations

Myosin binding protein C: Structural abnormalities in familial hypertrophic cardiomyopathy

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

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