Peptide competition of actin activation of myosin‐subfragment 1 ATPase by an amino terminal actin fragment

Kögler, Harald; Moir, Arthur J. G.; Trayer, Ian P.; Rüegg, J. C.

doi:10.1016/0014-5793(91)81336-7

Cited by 13 publications

(12 citation statements)

References 17 publications

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“…Indeed, using a zero-length cross-linking agent, Bertrand et al (1988) showed a strong proximity between sequence 87-113 and S-1 but the 82-119 fragment had no effect on the Mg2+-ATPase of S-1 (Kogler et al, 1991). Similar approaches have also illustrated the reactivity of GlulOO in this sequence (Elzinga, 1987 ;Vancompernolle et al, 1991).…”

Section: Discussionmentioning

confidence: 96%

“…(Moir et al, 1987) and immunochemical studies (Mkjean et al, 1987;Miller et al, 1987) have pin-pointed two actin segments in subdomain-1, residues 1-28 and 360-372, which are able to bind with the myosin head (Mtjean et al, 1987;Labbt et al, 1992). Synthetic peptide 1-28 is effective in myosin Mg2+-ATPase activation and includes two active portions located in the 1-14 and 18-28 sequences (Kogler et al, 1991;Van Eyk et al, 1991). It has also been implicated in the troponin-I interaction in the absence of Ca*+ (Levine et al, 1988;Van Eyk et al, 1991) and in caldesmon binding (Adams et al, 1990).…”

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confidence: 99%

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Localization of two myosin‐subfragment‐1 binding contacts in the 96–132 region of actin subdomain‐1

Labbé

Boyer

Méjea

et al. 1993

European Journal of Biochemistry

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Many direct observations and indirect experimental approaches have pin-pointed two segments (sequences 1-28 and 360-372) in actin subdomain-1 which bind to myosin subfragment-1. In a previous investigation [Labbt, J. P., Mtjean, C., Benyamin, Y. & Roustan, C. (1990) Biochem. J. 271, 407-4131, we have observed competition between myosin subfragment-1 and anti-actin antibodies specific to epitopes including Thrl03. A multisite interface model has also been proposed to take into account myosin-head binding to the N-terminal and C-terminal regions and to more central 40 -11 3 sequence of actin.In the present study, two limited actin segments encompassing residues 96-103 and 112-125 were identified as myosin-head-binding sites. The in vitro inhibitory effect of filamin on actin-activated Mg*+-ATPase would thus be explained by this competition. Furthermore, the (27-ma-50-kDa-20-kDa) trypsin-split myosin subfragment-1 which could no longer be activated by actin, did not bind at all to the two sites located in the 96-125 region, but it still interacted with the 360-372 segment.Our results regarding the position of the myosin head on actin monomers in rigor conditions provide evidence on the presence of two topologically independant contact points in the myosinheaaactin interface. One group exposed residues in the 1-7, 21-29, 77-95 and 96-103 actin segment, another, on the opposite side of subdomain-1. included residues from 112-125 and 360-372 sequences.Identification of the actidmyosin interface is essential in understanding the cyclical enzymic and mechanical process of myofibrillar contraction. Several indirect experimental approaches such as chemical cross-linking (Sutoh, 1982), NMR Correspondence to

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Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 99%

Localization of two myosin‐subfragment‐1 binding contacts in the 96–132 region of actin subdomain‐1

Labbé

Boyer

Méjea

et al. 1993

European Journal of Biochemistry

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“…While actin with the first 47 amino acids cleaved from the Nterminus is still able to bind myosin and activate its ATPase activity [154] albeit with reduced in vitro motility [153], the Nterminal peptide alone (amino acids 1-47) can also activate myosin ATPase [158,159]. The N-terminus forms contacts with myosin heavy chain [160,161] in the presence of nucleotide [161].…”

Section: Motility In Vitro and Myosin Bindingmentioning

confidence: 99%

Molecular genetics of actin function

Hennessey

Drummond

Sparrow

1993

Biochemical Journal

103

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“…The actin 1-28 interaction with S1 is pH sensitive (Van Eyk & Hodges, 1993): at pH 7.6, actin 1-28 induces approximately a 1.8-fold activation of SI . A longer actin fragment, residues 1-44, induces a 3.3-fold activation of the SI ATPase activity (Kogler et al, 1991). The actin peptides 1-28 and 1-44 and Mab B4 function as actin agonists.…”

Section: Discussionmentioning

confidence: 99%

“…It is an SI(Al)(A2) (-115,ooO Da) complex that is isolated from the chymotrypsin digestion of myosin. Like actin, a synthetic peptide actin 1-28 (Van Eyk & Hodges, 1991) and a longer enzymatic actin fragment, residues 1-44 (Kogler et al, 1991), are able to activate the S1 ATPase activity. The location of the TnI binding site for the N-terminus of actin has been identified at or near the inhibitory region of TnI, residues 96-116 (Grabarek & Gergely, 1987;Levine et al, 1988;.…”

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confidence: 99%

Anti‐peptide monoclonal antibody imaging of a common binding domain involved in muscle regulation

et al. 1995

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Multiple-component regulatory protein systems function through a generalized mechanism where a single regulatory protein or ligand binds to a variety of receptors to modulate specific functions in a physiologically sensitive context. Muscle contraction is regulated by the interaction of actin with troponin I (Tnl) or myosin in a Ca'+-sensitive manner. Actin utilizes a single binding domain (residues 1-28) to bind to residues 104-115 of TnI (Van Eyk JE, Sonnichsen FD, Sykes BD, Hodges RS, 1991, In: Riiegg JC, ed, Peptides us probes in muscle research, Heidelberg, Germany: Springer-Verlag, pp 15-31) and to myosin subfragment 1 (Sl, an enzymatic fragment of myosin containing both the actin and ATP binding sites) (Van Eyk JE, Hodges RS, 1991, Biochemisfry 30:11676-11682) in a Ca2+-sensitive manner. We have utilized an anti-TnI peptide (104-1 15) monoclonal antibody, Mab B4, that binds specifically to TnI, to image the common binding domain of actin and thus mimic the activity of actin including activation of the S1 ATPase activity and TnI-mediated regulation of the SI ATPase.Mab B4 has also been utilized to identify a receptor binding domain on myosin (residues 633-644) that is recognized by actin. Interestingly, Mab B4 binds to the native protein receptors TnI and S1 with relative affinities of 100-and 25,000-fold higher than the binding affinity to the 12-residue peptide immunogen. Thus, anti-peptide monoclonal antibodies prepared against a receptor binding domain can mimic the ligand binding domain and be utilized as a powerful tool for the detailed analysis of complex multiple-component regulatory systems.

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Peptide competition of actin activation of myosin‐subfragment 1 ATPase by an amino terminal actin fragment

Cited by 13 publications

References 17 publications

Localization of two myosin‐subfragment‐1 binding contacts in the 96–132 region of actin subdomain‐1

Localization of two myosin‐subfragment‐1 binding contacts in the 96–132 region of actin subdomain‐1

Molecular genetics of actin function

Anti‐peptide monoclonal antibody imaging of a common binding domain involved in muscle regulation

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