Determination of and corrections to sequences of turkey and chicken troponins-C. Effects of Thr-130 to Ile mutation on Ca2+ affinity

Golosinska, K; Pearlstone, Joyce R.; Borgford, Thor J.; Oikawa, Kimio; Kay, Cyril M.; Carpenter, Michael R.; Smillie, Lawrence B.

doi:10.1016/s0021-9258(18)98479-6

Cited by 56 publications

(78 citation statements)

References 34 publications

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“…fluorescent reporter of Ca 2ϩ binding to the N-terminal sites (Johnson et al, 1994). This protein, F29W, has the same Ca 2ϩ affinity as rTnC (Golosinska et al, 1991;Chandra et al, 1994) and presumably a similar Ca 2ϩ dissociation rate, which is similar to that for rabbit skeletal muscle TnC (Johnson et al, 1994). Thus some other factor must be involved in the small differences seen in Fig.…”

Section: Controlsmentioning

confidence: 86%

“…A spontaneous mutation in the cDNA that was cloned to produce the recombinant proteins originally led to replacement of Thr 130 (corresponding to Thr 127 in the rabbit protein) with Ile. In a previous report, this was shown to reduce the Ca 2ϩ affinity of the C-terminal sites by about 0.4 log units (Golosinska et al, 1991). For this reason, we tested the recombinant chicken protein I130T, which was constructed to restore the original Thr residue at position 130, and has normal Ca 2ϩ affinity (Golosinska et al, 1991).…”

Section: Controlsmentioning

confidence: 97%

“…The effects of replacing native rabbit TnC with chicken TnC were studied by comparing native TnC and the control rTnC with a TnC (I130T) that repairs a spontaneous mutation (T 130 3 I) occurring in the chicken cDNA clone (Golosinska et al, 1991). This control is presented at the end of the Results section.…”

Section: Tnc Extraction and Reconstitutionmentioning

confidence: 99%

“…The N-helix deleted recombinant protein NHdel, lacking residues 1-11, was produced by site-directed mutagenesis (Chandra et al, 1994), followed by expression and purification according to Golosinska et al (1991). Amino-terminal sequences of the control rTnC and NHdel were confirmed by automated Edman degradation methods.…”

Section: Proteinsmentioning

confidence: 99%

“…Amino-terminal sequences of the control rTnC and NHdel were confirmed by automated Edman degradation methods. The mutant I130T was constructed as described (Golosinska et al, 1991) and the entire cDNA of the coding region of the M13 vector was sequenced to confirm the structure (Fig. 1).…”

Section: Proteinsmentioning

confidence: 99%

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Regulation of Skeletal Muscle Tension Redevelopment by Troponin C Constructs with Different Ca2+ Affinities

Regnier

Rivera

Chase

et al. 1999

Biophysical Journal

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In maximally activated skinned fibers, the rate of tension redevelopment (ktr) following a rapid release and restretch is determined by the maximal rate of cross-bridge cycling. During submaximal Ca2+ activations, however, ktr regulation varies with thin filament dynamics. Thus, decreasing the rate of Ca2+ dissociation from TnC produces a higher ktr value at a given tension level (P), especially in the [Ca2+] range that yields less than 50% of maximal tension (Po). In this study, native rabbit TnC was replaced with chicken recombinant TnC, either wild-type (rTnC) or mutant (NHdel), with decreased Ca2+ affinity and an increased Ca2+ dissociation rate (koff). Despite marked differences in Ca2+ sensitivity (>0.5 DeltapCa50), fibers reconstituted with either of the recombinant proteins exhibited similar ktr versus tension profiles, with ktr low (1-2 s-1) and constant up to approximately 50% Po, then rising sharply to a maximum (16 +/- 0.8 s-1) in fully activated fibers. This behavior is predicted by a four-state model based on coupling between cross-bridge cycling and thin filament regulation, where Ca2+ directly affects only individual thin filament regulatory units. These data and model simulations confirm that the range of ktr values obtained with varying Ca2+ can be regulated by a rate-limiting thin filament process.

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Section: Controlsmentioning

confidence: 86%

Section: Controlsmentioning

confidence: 97%

Section: Tnc Extraction and Reconstitutionmentioning

confidence: 99%

Section: Proteinsmentioning

confidence: 99%

Section: Proteinsmentioning

confidence: 99%

See 3 more Smart Citations

Regulation of Skeletal Muscle Tension Redevelopment by Troponin C Constructs with Different Ca2+ Affinities

Regnier

Rivera

Chase

et al. 1999

Biophysical Journal

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TroponinC

Gagn��

2004

Handbook of Metalloproteins

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Regulation of contraction in skeletal and cardiac muscle occurs through calcium binding to the protein troponin C (TnC). The N‐terminal domain of TnC (NTnC) carries out the regulatory role through the binding of calcium ions – two calcium ions in skeletal muscle and one in cardiac muscle. Thirty‐nine sequences of TnC have been sequenced so far. Of the 39 sequences of TnC, 5 have had their three‐dimensional structures determined in various forms by NMR and X‐ray. Available structures include 26 uncomplexed structures in various calcium states, and 13 structures in which cardiac and skeletal TnC is complexed with fragments of troponin I and/or troponin T.

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TroponinC

Gagné

2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Determination of and corrections to sequences of turkey and chicken troponins-C. Effects of Thr-130 to Ile mutation on Ca2+ affinity

Cited by 56 publications

References 34 publications

Regulation of Skeletal Muscle Tension Redevelopment by Troponin C Constructs with Different Ca2+ Affinities

Regulation of Skeletal Muscle Tension Redevelopment by Troponin C Constructs with Different Ca2+ Affinities

TroponinC

TroponinC

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