Localization of the fast skeletal muscle troponin I gene (TNNI2) to 11p15.5: genes for troponin I and T are organized in pairs

Barton, Paul J.R.; Townsend, P. J.; Brand, Nigel J.; YACOUB, M. H.

doi:10.1017/s0003480097006556

Cited by 6 publications

(5 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The differential expression of SMYD 3 in duck may be related to greater myogenic potential. Troponin I2 ( TNNI 2), a muscle growth marker gene [ 67 , 68 ], encodes a subunit of troponin complex [ 69 ], which are expressed under muscle type-specific and developmental regulations [ 70 ]. Troponin complex is a group of muscle proteins, which is part of the contraction device of rapid skeletal muscle contraction [ 71 ].…”

Section: Discussionmentioning

confidence: 99%

Comparative Transcriptome Profiling of Skeletal Muscle from Black Muscovy Duck at Different Growth Stages Using RNA-seq

Cao

et al. 2020

Genes

View full text Add to dashboard Cite

In China, the production for duck meat is second only to that of chicken, and the demand for duck meat is also increasing. However, there is still unclear on the internal mechanism of regulating skeletal muscle growth and development in duck. This study aimed to identity candidate genes related to growth of duck skeletal muscle and explore the potential regulatory mechanism. RNA-seq technology was used to compare the transcriptome of skeletal muscles in black Muscovy ducks at different developmental stages (day 17, 21, 27, 31, and 34 of embryos and postnatal 6-month-olds). The SNPs and InDels of black Muscovy ducks at different growth stages were mainly in “INTRON”, “SYNONYMOUS_CODING”, “UTR_3_PRIME”, and “DOWNSTREAM”. The average number of AS in each sample was 37,267, mainly concentrated in TSS and TTS. Besides, a total of 19 to 5377 DEGs were detected in each pairwise comparison. Functional analysis showed that the DEGs were mainly involved in the processes of cell growth, muscle development, and cellular activities (junction, migration, assembly, differentiation, and proliferation). Many of DEGs were well known to be related to growth of skeletal muscle in black Muscovy duck, such as MyoG, FBXO1, MEF2A, and FoxN2. KEGG pathway analysis identified that the DEGs were significantly enriched in the pathways related to the focal adhesion, MAPK signaling pathway and regulation of the actin cytoskeleton. Some DEGs assigned to these pathways were potential candidate genes inducing the difference in muscle growth among the developmental stages, such as FAF1, RGS8, GRB10, SMYD3, and TNNI2. Our study identified several genes and pathways that may participate in the regulation of skeletal muscle growth in black Muscovy duck. These results should serve as an important resource revealing the molecular basis of muscle growth and development in duck.

show abstract

Section: Discussionmentioning

confidence: 99%

Comparative Transcriptome Profiling of Skeletal Muscle from Black Muscovy Duck at Different Growth Stages Using RNA-seq

Cao

et al. 2020

Genes

View full text Add to dashboard Cite

show abstract

“…The stoichiometry of TnT binding to F-actin is in a ratio of 1 (TnT) to 7 (actin monomers) (al-Hillawi, Bhandari et al 1995). During the last two decades, extensive studies revealed that vertebrate TnT is encoded by three homologous genes that specifically expressed in slow skeletal muscle ( TNNT1 ), cardiac muscle ( TNNT2 ), and fast skeletal muscle ( TNNT3 ) (Barton, Townsend et al 1997) (Table 1). …”

Section: Introductionmentioning

confidence: 99%

TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and structure–function relationships

Wei

Jin

2016

Gene

171

144

View full text Add to dashboard Cite

Troponin T (TnT) is a central player in the calcium regulation of actin thin filament function and is essential for the contraction of striated muscles. Three homologous genes have evolved in vertebrates to encode three muscle type-specific TnT isoforms: TNNT1 for slow skeletal muscle TnT, TNNT2 for cardiac muscle TnT, and TNNT3 for fast skeletal muscle TnT. Alternative splicing and posttranslational modifications confer additional structural and functional variations of TnT during development and muscle adaptation to various physiological and pathological conditions. This review focuses on the TnT isoform genes and their molecular evolution, alternative splicing, developmental regulation, structure-function relationships of TnT proteins, posttranslational modifications, and myopathic mutations and abnormal splicing. The goal is to provide a concise summary of the current knowledge and some perspectives for future research and translational applications.

show abstract

“…1B) and genes encoding TnI and TnT are closely linked in the vertebrate genome (Huang and Jin, 1999), suggesting their origin from the duplication of a single ancestral gene followed by neofunctionalization. As linked pairs of genes, TnI and TnT have each evolved into three isoforms with specific expressions in cardiac, slow and fast skeletal muscles (Barton et al, 1997; Tiso et al, 1997; Huang and Jin, 1999; Perry, 1998; 1999) (Fig. 1C), implying a series of duplication events from an ancestral TnI-TnT gene pair followed by subfunctionization and neofunctionalization.…”

Section: Introductionmentioning

confidence: 99%

To Investigate Protein Evolution by Detecting Suppressed Epitope Structures

2009

View full text Add to dashboard Cite

Material remains of ancestor nucleotides and proteins are largely unavailable, thus sequence comparison among homologous genes in present-day organisms forms the core of current knowledge of molecular evolution. Variation in protein three-dimensional structure is a basis for functional diversity. To study the evolution of three-dimensional structures in related proteins would significantly improve our understanding of protein evolution and function. A protein may contain ancestor conformations that have been allosterically suppressed by evolutionarily additive structures. Using monoclonal antibody probes to detect such conformation in proteins after removing the suppressor structure, our study demonstrated three-dimensional structure evidence for the evolutionary relationship between troponin I and troponin T, two subunits of the troponin complex in the Ca2+-regulatory system of striated muscle, and among their muscle type-specific isoforms. The experimental data showed the feasibility to detect evolutionarily suppressed history-telling structural states in proteins by removing conformational modulator segments added during evolution. In addition to identifying structural modifications that were critical to the emerging of diverged proteins, investigating this novel mode of evolution will help to understand the origin and functional potential of protein structures.

show abstract

Localization of the fast skeletal muscle troponin I gene (TNNI2) to 11p15.5: genes for troponin I and T are organized in pairs

Cited by 6 publications

References 0 publications

Comparative Transcriptome Profiling of Skeletal Muscle from Black Muscovy Duck at Different Growth Stages Using RNA-seq

Comparative Transcriptome Profiling of Skeletal Muscle from Black Muscovy Duck at Different Growth Stages Using RNA-seq

TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and structure–function relationships

To Investigate Protein Evolution by Detecting Suppressed Epitope Structures

Contact Info

Product

Resources

About