Molecular cloning of troponin I expressed in fast white muscle of a teleost fish, the Atlantic herring (Clupea harengus L.)

Hodgson, Paula; Leaver, Michael J.; George, Stephen; MacLean, Darren W.; Hastings, Kenneth E.M.

doi:10.1016/0167-4781(96)00033-4

Cited by 8 publications

(5 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Three genes code for slow, fast and cardiac isoforms of TnI in birds and mammals (Guenet et al, 1996;Mullen and Barton, Table·3 (Jackman et al, 1998) and one from herring (Hodgson et al, 1996). Surprisingly, however, in each case the amino acid sequence identity was considered too low to assign orthology to either the fast, slow or cardiac varieties seen in other vertebrates.…”

Section: Discussionmentioning

confidence: 99%

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

Hall

Cole

Johnston

2003

Journal of Experimental Biology

View full text Add to dashboard Cite

SUMMARYSeven cDNA clones coding for different muscle-specific proteins (MSPs) were isolated from the fast muscle tissue of Atlantic cod Gadus morhua L. In situ hybridization using cRNA probes was used to characterize the temporal and spatial patterns of gene expression with respect to somite stage in embryos incubated at 4°C, 7°C and 10°C. MyoDtranscripts were first observed in the presomitic mesoderm prior to somite formation, and in the lateral compartment of the forming somites. MyoD expression was not observed in the adaxial cells that give rise to the slow muscle layer, and expression was undetectable by in situhybridization in the lateral somitic mesoderm after the 35-somite stage,during development of the final ∼15 somites. RT-PCR analysis, however,confirmed the presence of low levels of the transcript during these later stages. A phylogenetic comparison of the deduced aminoacid sequences of the full-length MyoD cDNA clone and those from other teleosts, and inference from the in situ expression pattern suggested homology with a second paralogue (MyoD2) recently isolated from the gilthead seabream Sparus aurata. Following MyoD expression,α-actin was the first structural gene to be switched on at the 16-somite stage, followed by myosin heavy chain, troponin T, troponin I and muscle creatine kinase. The final mRNA in the series to be expressed was troponin C. All genes were switched on prior to myofibril assembly. The troponin C sequence was unusual in that it showed the greatest sequence identity with the rainbow trout Oncorhynchus mykiss cardiac/slow form, but was expressed in the fast myotomal muscle and not in the heart. In addition, the third TnC calcium binding site showed a lower level of sequence conservation than the rest of the sequence. No differences were seen in the timing of appearance or rate of posterior progression (relative to somite stage) of any MSP transcripts between embryos raised at the different temperatures. It was concluded that myofibrillar genes are activated asynchronously in a distinct temporal order prior to myofibrillar assembly and that this process was highly canalized over the temperature range studied.

show abstract

Section: Discussionmentioning

confidence: 99%

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

Hall

Cole

Johnston

2003

Journal of Experimental Biology

View full text Add to dashboard Cite

show abstract

“…The amino acid sequence of zebrafish TnnI2 exhibited a high degree of identity to that of quail (Baldwin et al, 1985), mice (Koppe et al, 1989), humans (Zhu et al, 1994), amphibian (Warkman and Atkinson, 2002) and fish (Hodgson et al, 1996 andJackman et al, 1998). In mammals, the expression of TnnI2 is in skeletal muscle (Trimmer et al, 1989), but it is not expressed in heart.…”

Section: Spatial Expression Of Tnni2 In Zebrafish Embryosmentioning

confidence: 99%

The molecular structures and expression patterns of zebrafish troponin I genes

Tsai

2009

Gene Expression Patterns

View full text Add to dashboard Cite

“…The expression of TnI isoforms is regulated in different muscle types and during development ( , ). Primary structures of cardiac, fast, and slow skeletal muscle TnI isoforms have been determined in a number of species ( − ). The main structural difference between cardiac and skeletal muscle TnI is an NH 2 -terminal extension unique to cardiac TnI (cTnI), containing phosphorylation sites for cAMP-dependent protein kinase (PKA) ().…”

mentioning

confidence: 99%

The Highly Conserved COOH Terminus of Troponin I Forms a Ca²⁺-Modulated Allosteric Domain in the Troponin Complex

Jin

Yang

et al. 2001

Biochemistry

View full text Add to dashboard Cite

The primary structure of the COOH-terminal region of troponin I (TnI) is highly conserved among the cardiac, slow, and fast skeletal muscle TnI isoforms and across species. Although no binding site for the other thin filament proteins is found at the COOH terminus of TnI, truncations of the last 19-23 amino acid residues reduce the activity of TnI in the inhibition of actomyosin ATPase and result in cardiac muscle malfunction. We have developed a specific monoclonal antibody (mAb), TnI-1, against the conserved COOH terminus of TnI. Using this mAb, isolation of the troponin complex by immunoaffinity chromatography from muscle homogenate and immunofluorescence microscopic staining of myofibrils indicate that the COOH terminus of TnI forms an exposed structure in the muscle thin filament. Binding of this mAb to the COOH terminus of cardiac TnI induced extensive conformational changes in the protein, suggesting an allosteric role of this region in the functional integrity of troponin. In the absence of Ca2+, the binding of troponin C and troponin T to TnI had very little effect on the conformation of the COOH terminus of TnI as indicated by the unaffected mAb affinity for the TnI-1 epitope. However, Ca2+ significantly increased the accessibility of the TnI-1 epitope on TnI in the presence of troponin C and troponin T. The results provide evidence that the COOH terminus is an essential structure in TnI and participates in the allosteric switch during Ca2+ activation of contraction.

show abstract

Molecular cloning of troponin I expressed in fast white muscle of a teleost fish, the Atlantic herring (Clupea harengus L.)

Cited by 8 publications

References 15 publications

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

The molecular structures and expression patterns of zebrafish troponin I genes

The Highly Conserved COOH Terminus of Troponin I Forms a Ca²⁺-Modulated Allosteric Domain in the Troponin Complex

Contact Info

Product

Resources

About

Molecular cloning of troponin I expressed in fast white muscle of a teleost fish, the Atlantic herring (Clupea harengus L.)

Cited by 8 publications

References 15 publications

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

The molecular structures and expression patterns of zebrafish troponin I genes

The Highly Conserved COOH Terminus of Troponin I Forms a Ca2+-Modulated Allosteric Domain in the Troponin Complex

Contact Info

Product

Resources

About

The Highly Conserved COOH Terminus of Troponin I Forms a Ca²⁺-Modulated Allosteric Domain in the Troponin Complex