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Journal articles on the topic 'Drosophila Troponin I'

Author: Grafiati

Published: 6 September 2023

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1

QIU, Feng, Anne LAKEY, Bogos AGIANIAN, et al. "Troponin C in different insect muscle types: identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect." Biochemical Journal 371, no. 3 (2003): 811–21. http://dx.doi.org/10.1042/bj20021814.

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The indirect flight muscles (IFMs) of Lethocerus (giant water bug) and Drosophila (fruitfly) are asynchronous: oscillatory contractions are produced by periodic stretches in the presence of a Ca2+ concentration that does not fully activate the muscle. The troponin complex on thin filaments regulates contraction in striated muscle. The complex in IFM has subunits that are specific to this muscle type, and stretch activation may act through troponin. Lethocerus and Drosophila have an unusual isoform of the Ca2+-binding subunit of troponin, troponin C (TnC), with a single Ca2+-binding site near t

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2

Terami, Hiromi, Benjamin D. Williams, Shin-ichi Kitamura, et al. "Genomic Organization, Expression, and Analysis of the Troponin C Gene pat-10 of Caenorhabditis elegans." Journal of Cell Biology 146, no. 1 (1999): 193–202. http://dx.doi.org/10.1083/jcb.146.1.193.

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We have cloned and characterized the troponin C gene, pat-10 of the nematode Caenorhabditis elegans. At the amino acid level nematode troponin C is most similar to troponin C of Drosophila (45% identity) and cardiac troponin C of vertebrates. Expression studies demonstrate that this troponin is expressed in body wall muscle throughout the life of the animal. Later, vulval muscles and anal muscles also express this troponin C isoform. The structural gene for this troponin is pat-10 and mutations in this gene lead to animals that arrest as twofold paralyzed embryos late in development. We have s

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3

Mas, José-Antonio, Elena García-Zaragoza, and Margarita Cervera. "Two Functionally Identical Modular Enhancers in Drosophila Troponin T Gene Establish the Correct Protein Levels in Different Muscle Types." Molecular Biology of the Cell 15, no. 4 (2004): 1931–45. http://dx.doi.org/10.1091/mbc.e03-10-0729.

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The control of muscle-specific expression is one of the principal mechanisms by which diversity is generated among muscle types. In an attempt to elucidate the regulatory mechanisms that control fiber diversity in any given muscle, we have focused our attention on the transcriptional regulation of the Drosophila Troponin T gene. Two, nonredundant, functionally identical, enhancer-like elements activate Troponin T transcription independently in all major muscles of the embryo and larvae as well as in adult somatic and visceral muscles. Here, we propose that the differential but concerted intera

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4

Beall, C. J., and E. Fyrberg. "Muscle abnormalities in Drosophila melanogaster heldup mutants are caused by missing or aberrant troponin-I isoforms." Journal of Cell Biology 114, no. 5 (1991): 941–51. http://dx.doi.org/10.1083/jcb.114.5.941.

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We have investigated the molecular bases of muscle abnormalities in four Drosophila melanogaster heldup mutants. We find that the heldup gene encodes troponin-I, one of the principal regulatory proteins associated with skeletal muscle thin filaments. heldup3, heldup4, and heldup5 mutants, all of which have grossly abnormal flight muscle myofibrils, lack mRNAs encoding one or more troponin-I isoforms. In contrast, heldup2, an especially interesting mutant wherein flight muscles are atrophic, synthesizes the complete mRNA complement. By sequencing mutant troponin-I cDNAs we demonstrate that the

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5

Nongthomba, Upendra, Mark Cummins, Samantha Clark, Jim O. Vigoreaux, and John C. Sparrow. "Suppression of Muscle Hypercontraction by Mutations in the Myosin Heavy Chain Gene of Drosophila melanogaster." Genetics 164, no. 1 (2003): 209–22. http://dx.doi.org/10.1093/genetics/164.1.209.

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Abstract The indirect flight muscles (IFM) of Drosophila melanogaster provide a good genetic system with which to investigate muscle function. Flight muscle contraction is regulated by both stretch and Ca2+-induced thin filament (actin + tropomyosin + troponin complex) activation. Some mutants in troponin-I (TnI) and troponin-T (TnT) genes cause a “hypercontraction” muscle phenotype, suggesting that this condition arises from defects in Ca2+ regulation and actomyosin-generated tension. We have tested the hypothesis that missense mutations of the myosin heavy chain gene, Mhc, which suppress the

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6

Marín, María-Cruz, José-Rodrigo Rodríguez, and Alberto Ferrús. "Transcription of Drosophila Troponin I Gene Is Regulated by Two Conserved, Functionally Identical, Synergistic Elements." Molecular Biology of the Cell 15, no. 3 (2004): 1185–96. http://dx.doi.org/10.1091/mbc.e03-09-0663.

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The Drosophila wings-up A gene encodes Troponin I. Two regions, located upstream of the transcription initiation site (upstream regulatory element) and in the first intron (intron regulatory element), regulate gene expression in specific developmental and muscle type domains. Based on LacZ reporter expression in transgenic lines, upstream regulatory element and intron regulatory element yield identical expression patterns. Both elements are required for full expression levels in vivo as indicated by quantitative reverse transcription-polymerase chain reaction assays. Three myocyte enhancer fac

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7

Chechenova, Maria B., Sara Maes, Sandy T. Oas, et al. "Functional redundancy and nonredundancy between two Troponin C isoforms inDrosophilaadult muscles." Molecular Biology of the Cell 28, no. 6 (2017): 760–70. http://dx.doi.org/10.1091/mbc.e16-07-0498.

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We investigated the functional overlap of two muscle Troponin C (TpnC) genes that are expressed in the adult fruit fly, Drosophila melanogaster: TpnC4 is predominantly expressed in the indirect flight muscles (IFMs), whereas TpnC41C is the main isoform in the tergal depressor of the trochanter muscle (TDT; jump muscle). Using CRISPR/Cas9, we created a transgenic line with a homozygous deletion of TpnC41C and compared its phenotype to a line lacking functional TpnC4. We found that the removal of either of these genes leads to expression of the other isoform in both muscle types. The switching b

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8

Vicente-Crespo, Marta, Maya Pascual, Juan M. Fernandez-Costa, et al. "Drosophila Muscleblind Is Involved in troponin T Alternative Splicing and Apoptosis." PLoS ONE 3, no. 2 (2008): e1613. http://dx.doi.org/10.1371/journal.pone.0001613.

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9

Naimi, Benyoussef, Andrew Harrison, Mark Cummins, et al. "A Tropomyosin-2 Mutation Suppresses a Troponin I Myopathy inDrosophila." Molecular Biology of the Cell 12, no. 5 (2001): 1529–39. http://dx.doi.org/10.1091/mbc.12.5.1529.

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A suppressor mutation, D53, of theheld-up 2 allele of the Drosophila melanogaster Troponin I (wupA) gene is described. D53, a missense mutation, S185F, of the tropomyosin-2,Tm2, gene fully suppresses all the phenotypic effects ofheld-up 2, including the destructive hypercontraction of the indirect flight muscles (IFMs), a lack of jumping, the progressive myopathy of the walking muscles, and reductions in larval crawling and feeding behavior. The suppressor restores normal function of the IFMs, but flight ability decreases with age and correlates with an unusual, progressive structural collapse

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10

Montana, Enrico S., and J. Troy Littleton. "Characterization of a hypercontraction-induced myopathy in Drosophila caused by mutations in Mhc." Journal of Cell Biology 164, no. 7 (2004): 1045–54. http://dx.doi.org/10.1083/jcb.200308158.

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The Myosin heavy chain (Mhc) locus encodes the muscle-specific motor mediating contraction in Drosophila. In a screen for temperature-sensitive behavioral mutants, we have identified two dominant Mhc alleles that lead to a hypercontraction-induced myopathy. These mutants are caused by single point mutations in the ATP binding/hydrolysis domain of Mhc and lead to degeneration of the flight muscles. Electrophysiological analysis in the adult giant fiber flight circuit demonstrates temperature-dependent seizure activity that requires neuronal input, as genetic blockage of neuronal activity suppre

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11

Kronert, William A., Angel Acebes, Alberto Ferrús, and Sanford I. Bernstein. "Specific Myosin Heavy Chain Mutations Suppress Troponin I Defects in Drosophila Muscles." Journal of Cell Biology 144, no. 5 (1999): 989–1000. http://dx.doi.org/10.1083/jcb.144.5.989.

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We show that specific mutations in the head of the thick filament molecule myosin heavy chain prevent a degenerative muscle syndrome resulting from the hdp2 mutation in the thin filament protein troponin I. One mutation deletes eight residues from the actin binding loop of myosin, while a second affects a residue at the base of this loop. Two other mutations affect amino acids near the site of nucleotide entry and exit in the motor domain. We document the degree of phenotypic rescue each suppressor permits and show that other point mutations in myosin, as well as null mutations, fail to suppre

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12

Herranz, R. "Expression patterns of the whole Troponin C gene repertoire during Drosophila development." Gene Expression Patterns 4, no. 2 (2004): 183–90. http://dx.doi.org/10.1016/j.modgep.2003.09.008.

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13

SINGH, SALAM HEROJEET, PRABODH KUMAR, NALLUR B. RAMACHANDRA, and UPENDRA NONGTHOMBA. "Roles of the troponin isoforms during indirect flight muscle development in Drosophila." Journal of Genetics 93, no. 2 (2014): 379–88. http://dx.doi.org/10.1007/s12041-014-0386-8.

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14

Fyrberg, Eric, Christine C. Fyrberg, Clifford Beall, and Donna L. Saville. "Drosophila melanogaster troponin-T mutations engender three distinct syndromes of myofibrillar abnormalities." Journal of Molecular Biology 216, no. 3 (1990): 657–75. http://dx.doi.org/10.1016/0022-2836(90)90390-8.

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15

Cao, Tianxin, Alyson Sujkowski, Tyler Cobb, Robert J. Wessells, and Jian-Ping Jin. "The glutamic acid-rich–long C-terminal extension of troponin T has a critical role in insect muscle functions." Journal of Biological Chemistry 295, no. 12 (2020): 3794–807. http://dx.doi.org/10.1074/jbc.ra119.012014.

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The troponin complex regulates the Ca2+ activation of myofilaments during striated muscle contraction and relaxation. Troponin genes emerged 500–700 million years ago during early animal evolution. Troponin T (TnT) is the thin-filament–anchoring subunit of troponin. Vertebrate and invertebrate TnTs have conserved core structures, reflecting conserved functions in regulating muscle contraction, and they also contain significantly diverged structures, reflecting muscle type- and species-specific adaptations. TnT in insects contains a highly-diverged structure consisting of a long glutamic acid–r

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16

Fyrberg, Christine, Heather Parker, Bernadette Hutchison, and Eric Fyrberg. "Drosophila melanogaster genes encoding three troponin-C isoforms and a calmodulin-related protein." Biochemical Genetics 32, no. 3-4 (1994): 119–35. http://dx.doi.org/10.1007/bf00554420.

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17

PECKHAM, MICHELLE, RICHARD CRIPPS, DAVID WHITE, and BELINDA BULLARD. "Mechanics and Protein Content of Insect Flight Muscles." Journal of Experimental Biology 168, no. 1 (1992): 57–76. http://dx.doi.org/10.1242/jeb.168.1.57.

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In asynchronous insect flight muscles, stretch activation may arise from a matching of the helix periodicities of actin target sites to myosin heads and/or a special form of troponin subunit called troponin-H (Tn-H, relative molecular mass 80×103), which has so far only been found in the asynchronous flight muscles of Drosophila (Diptera) and Lethocerus (Hemiptera). The sequence of Tn-H in Drosophila shows it to be a fusion protein of tropomyosin and a hydrophobic proline-rich sequence. Tn-H in Lethocerus is immunologically similar. From immunoblots of synchronous (non-stretch-activated) and a

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18

Barbas, J. A., J. Galceran, I. Krah-Jentgens, et al. "Troponin I is encoded in the haplolethal region of the Shaker gene complex of Drosophila." Genes & Development 5, no. 1 (1991): 132–40. http://dx.doi.org/10.1101/gad.5.1.132.

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19

Prado, A., I. Canal, J. A. Barbas, J. Molloy, and A. Ferrús. "Functional recovery of troponin I in a Drosophila heldup mutant after a second site mutation." Molecular Biology of the Cell 6, no. 11 (1995): 1433–41. http://dx.doi.org/10.1091/mbc.6.11.1433.

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To identify proteins that interact in vivo with muscle components we have used a genetic approach based on the isolation of suppressors of mutant alleles of known muscle components. We have applied this system to the case of troponin I (TnI) in Drosophila and its mutant allele heldup2 (hdp2). This mutation causes an alanine to valine substitution at position 116 after a single nucleotide change in a constitutive exon. Among the isolated suppressors, one of them results from a second site mutation at the TnI gene itself. Muscles endowed with TnI mutated at both sites support nearly normal myofi

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20

Eldred, Catherine C., Anja Katzemich, Georgia Yalanis, Andrea Page-McCaw, Belinda Bullard, and Douglas Swank. "The Influence of Troponin C, Isoform 4 on Drosophila Development, Stretch Activation, and Power Generation." Biophysical Journal 102, no. 3 (2012): 155a. http://dx.doi.org/10.1016/j.bpj.2011.11.849.

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21

Eldred, Catherine C., Anja Katzemich, Monica Patel, Belinda Bullard, and Douglas M. Swank. "The roles of troponin C isoforms in the mechanical function of Drosophila indirect flight muscle." Journal of Muscle Research and Cell Motility 35, no. 3-4 (2014): 211–23. http://dx.doi.org/10.1007/s10974-014-9387-8.

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22

Glasheen, Bernadette M., Catherine C. Eldred, Leah C. Sullivan, et al. "Stretch activation properties of Drosophila and Lethocerus indirect flight muscle suggest similar calcium-dependent mechanisms." American Journal of Physiology-Cell Physiology 313, no. 6 (2017): C621—C631. http://dx.doi.org/10.1152/ajpcell.00110.2017.

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Muscle stretch activation (SA) is critical for optimal cardiac and insect indirect flight muscle (IFM) power generation. The SA mechanism has been investigated for decades with many theories proposed, but none proven. One reason for the slow progress could be that multiple SA mechanisms may have evolved in multiple species or muscle types. Laboratories studying IFM SA in the same or different species have reported differing SA functional properties which would, if true, suggest divergent mechanisms. However, these conflicting results might be due to different experimental methodologies. Thus,

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23

MARCO-FERRERES, Raquel, Juan J. ARREDONDO, Benito FRAILE, and Margarita CERVERA. "Overexpression of troponin T in Drosophila muscles causes a decrease in the levels of thin-filament proteins." Biochemical Journal 386, no. 1 (2005): 145–52. http://dx.doi.org/10.1042/bj20041240.

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Formation of the contractile apparatus in muscle cells requires co-ordinated activation of several genes and the proper assembly of their products. To investigate the role of TnT (troponin T) in the mechanisms that control and co-ordinate thin-filament formation, we generated transgenic Drosophila lines that overexpress TnT in their indirect flight muscles. All flies that overexpress TnT were unable to fly, and the loss of thin filaments themselves was coupled with ultrastructural perturbations of the sarcomere. In contrast, thick filaments remained largely unaffected. Biochemical analysis of

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24

Nongthomba, Upendra, Maqsood Ansari, Divesh Thimmaiya, Meg Stark, and John Sparrow. "Aberrant Splicing of an Alternative Exon in the Drosophila Troponin-T Gene Affects Flight Muscle Development." Genetics 177, no. 1 (2007): 295–306. http://dx.doi.org/10.1534/genetics.106.056812.

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25

Gajewski, Kathleen M., Jianbo Wang, and Robert A. Schulz. "Calcineurin function is required for myofilament formation and troponin I isoform transition in Drosophila indirect flight muscle." Developmental Biology 289, no. 1 (2006): 17–29. http://dx.doi.org/10.1016/j.ydbio.2005.09.039.

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26

Casas-Tintó, Sergio, and Alberto Ferrús. "The haplolethality paradox of the wupA gene in Drosophila." PLOS Genetics 17, no. 3 (2021): e1009108. http://dx.doi.org/10.1371/journal.pgen.1009108.

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Haplolethals (HL) are regions of diploid genomes that in one dose are fatal for the organism. Their biological meaning is obscure because heterozygous loss-of-function mutations result in dominant lethality (DL) and, consequently, should be under strong negative selection. We report an in depth study of the HL associated to the gene wings up A (wupA). It encodes 13 transcripts (A-M) that yield 11 protein isoforms (A-K) of Troponin I (TnI). They are functionally diverse in their control of muscle contraction, cell polarity and cell proliferation. Isoform K transfers to the nucleus where it incr

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27

Cozhimuttam Viswanathan, Meera, William Lehman, and Anthony Cammarato. "A Troponin-T Mutation Initiates Cardiac and Skeletal Myopathy due to Impaired Inhibition of Contraction in Drosophila Melanogaster." Biophysical Journal 104, no. 2 (2013): 311a. http://dx.doi.org/10.1016/j.bpj.2012.11.1727.

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28

Prado, Antonio, Inmaculada Canal, and Alberto Ferrús. "The Haplolethal Region at the 16F Gene Cluster of Drosophila melanogaster: Structure and Function." Genetics 151, no. 1 (1999): 163–75. http://dx.doi.org/10.1093/genetics/151.1.163.

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Abstract Extensive aneuploid analyses had shown the existence of a few haplolethal (HL) regions and one triplolethal region in the genome of Drosophila melanogaster. Since then, only two haplolethals, 22F1-2 and 16F, have been directly linked to identified genes, dpp and wupA, respectively. However, with the possible exception of dpp, the actual bases for this dosage sensitivity remain unknown. We have generated and characterized dominant-lethal mutations and chromosomal rearrangements in 16F and studied them in relation to the genes in the region. This region extends along 100 kb and includes

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29

Barbas, J. A., J. Galceran, L. Torroja, A. Prado, and A. Ferrús. "Abnormal muscle development in the heldup3 mutant of Drosophila melanogaster is caused by a splicing defect affecting selected troponin I isoforms." Molecular and Cellular Biology 13, no. 3 (1993): 1433–39. http://dx.doi.org/10.1128/mcb.13.3.1433-1439.1993.

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The troponin I (TnI) gene of Drosophila melanogaster encodes a family of 10 isoforms resulting from the differential splicing of 13 exons. Four of these exons (6a1, 6a2, 6b1, and 6b2) are mutually exclusive and very similar in sequence. TnI isoforms show qualitative specificity whereby each muscle expresses a selected repertoire of them. In addition, TnI isoforms show quantitative specificity whereby each muscle expresses characteristic amounts of each isoform. In the mutant heldup3, the development of the thoracic muscles DLM, DVM, and TDT is aborted. The mutation consists of a one-nucleotide

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30

Barbas, J. A., J. Galceran, L. Torroja, A. Prado, and A. Ferrús. "Abnormal muscle development in the heldup3 mutant of Drosophila melanogaster is caused by a splicing defect affecting selected troponin I isoforms." Molecular and Cellular Biology 13, no. 3 (1993): 1433–39. http://dx.doi.org/10.1128/mcb.13.3.1433.

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The troponin I (TnI) gene of Drosophila melanogaster encodes a family of 10 isoforms resulting from the differential splicing of 13 exons. Four of these exons (6a1, 6a2, 6b1, and 6b2) are mutually exclusive and very similar in sequence. TnI isoforms show qualitative specificity whereby each muscle expresses a selected repertoire of them. In addition, TnI isoforms show quantitative specificity whereby each muscle expresses characteristic amounts of each isoform. In the mutant heldup3, the development of the thoracic muscles DLM, DVM, and TDT is aborted. The mutation consists of a one-nucleotide

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31

Wang, Shuoshuo, Elizabeth Stoops, Unnikannan CP, et al. "Mechanotransduction via the LINC complex regulates DNA replication in myonuclei." Journal of Cell Biology 217, no. 6 (2018): 2005–18. http://dx.doi.org/10.1083/jcb.201708137.

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Nuclear mechanotransduction has been implicated in the control of chromatin organization; however, its impact on functional contractile myofibers is unclear. We found that deleting components of the linker of nucleoskeleton and cytoskeleton (LINC) complex in Drosophila melanogaster larval muscles abolishes the controlled and synchronized DNA endoreplication, typical of nuclei across myofibers, resulting in increased and variable DNA content in myonuclei of individual myofibers. Moreover, perturbation of LINC-independent mechanical input after knockdown of β-Integrin in larval muscles similarly

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32

Firdaus, H., J. Mohan, S. Naz, P. Arathi, S. R. Ramesh, and U. Nongthomba. "A cis-Regulatory Mutation in Troponin-I of Drosophila Reveals the Importance of Proper Stoichiometry of Structural Proteins During Muscle Assembly." Genetics 200, no. 1 (2015): 149–65. http://dx.doi.org/10.1534/genetics.115.175604.

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33

Chechenova, Maria B., Sara Maes, and Richard M. Cripps. "Expression of the Troponin C at 41C Gene in Adult Drosophila Tubular Muscles Depends upon Both Positive and Negative Regulatory Inputs." PLOS ONE 10, no. 12 (2015): e0144615. http://dx.doi.org/10.1371/journal.pone.0144615.

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34

Nikonova, Elena, Amartya Mukherjee, Ketaki Kamble, Christiane Barz, Upendra Nongthomba, and Maria L. Spletter. "Rbfox1 is required for myofibril development and maintaining fiber type–specific isoform expression in Drosophila muscles." Life Science Alliance 5, no. 4 (2022): e202101342. http://dx.doi.org/10.26508/lsa.202101342.

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Protein isoform transitions confer muscle fibers with distinct properties and are regulated by differential transcription and alternative splicing. RNA-binding Fox protein 1 (Rbfox1) can affect both transcript levels and splicing, and is known to contribute to normal muscle development and physiology in vertebrates, although the detailed mechanisms remain obscure. In this study, we report that Rbfox1 contributes to the generation of adult muscle diversity in Drosophila. Rbfox1 is differentially expressed among muscle fiber types, and RNAi knockdown causes a hypercontraction phenotype that lead

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35

Schultheiss, T. M., S. Xydas, and A. B. Lassar. "Induction of avian cardiac myogenesis by anterior endoderm." Development 121, no. 12 (1995): 4203–14. http://dx.doi.org/10.1242/dev.121.12.4203.

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An experimental system was devised to study the mechanisms by which cells become committed to the cardiac myocyte lineage during avian development. Chick tissues from outside the fate map of the heart (in the posterior primitive streak (PPS) of a Hamburger & Hamilton stage 4 embryo) were combined with potential inducing tissues from quail embryos and cultured in vitro. Species-specific RT-PCR was employed to detect the appearance of the cardiac muscle markers chick Nkx-2.5 (cNkx-2.5), cardiac troponin C and ventricular myosin heavy chain in the chick responder tissues. Using this procedure

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36

Coulter, L. R., M. A. Landree, and T. A. Cooper. "Identification of a new class of exonic splicing enhancers by in vivo selection." Molecular and Cellular Biology 17, no. 4 (1997): 2143–50. http://dx.doi.org/10.1128/mcb.17.4.2143.

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In vitro selection strategies have typically been used to identify a preferred ligand, usually an RNA, for an identified protein. Ideally, one would like to know RNA consensus sequences preferred in vivo for as-yet-unidentified factors. The ability to select RNA-processing signals would be particularly beneficial in the analysis of exon enhancer sequences that function in exon recognition during pre-mRNA splicing. Exon enhancers represent a class of potentially ubiquitous RNA-processing signals whose actual prevalence is unknown. To establish an approach for in vivo selection, we developed an

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37

Strehler, E. E., M. Periasamy, M. A. Strehler-Page, and B. Nadal-Ginard. "Myosin light-chain 1 and 3 gene has two structurally distinct and differentially regulated promoters evolving at different rates." Molecular and Cellular Biology 5, no. 11 (1985): 3168–82. http://dx.doi.org/10.1128/mcb.5.11.3168-3182.1985.

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DNA fragments located 10 kilobases apart in the genome and containing, respectively, the first myosin light chain 1 (MLC1f) and the first myosin light chain 3 (MLC3f) specific exon of the rat myosin light chain 1 and 3 gene, together with several hundred base pairs of upstream flanking sequences, have been shown in runoff in vitro transcription assays to direct initiation of transcription at the cap sites of MLC1f and MLC3f mRNAs used in vivo. These results establish the presence of two separate, functional promoters within that gene. A comparison of the nucleotide sequence of the rat MLC1f/3f

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38

Strehler, E. E., M. Periasamy, M. A. Strehler-Page, and B. Nadal-Ginard. "Myosin light-chain 1 and 3 gene has two structurally distinct and differentially regulated promoters evolving at different rates." Molecular and Cellular Biology 5, no. 11 (1985): 3168–82. http://dx.doi.org/10.1128/mcb.5.11.3168.

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DNA fragments located 10 kilobases apart in the genome and containing, respectively, the first myosin light chain 1 (MLC1f) and the first myosin light chain 3 (MLC3f) specific exon of the rat myosin light chain 1 and 3 gene, together with several hundred base pairs of upstream flanking sequences, have been shown in runoff in vitro transcription assays to direct initiation of transcription at the cap sites of MLC1f and MLC3f mRNAs used in vivo. These results establish the presence of two separate, functional promoters within that gene. A comparison of the nucleotide sequence of the rat MLC1f/3f

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39

Eldred, Catherine J., Laura Koppes, Kevin Georgek, Andrea Page-McCaw, Belinda Bullard, and Douglas M. Swank. "The Influence of Troponin C Isoforms on Drosophils Stretch Activation and Power Generation." Biophysical Journal 100, no. 3 (2011): 113a. http://dx.doi.org/10.1016/j.bpj.2010.12.824.

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40

Singh, Salam Herojeet, Prabodh Kumar, Nallur B. Ramachandra, and Upendra Nongthomba. "Correction to: Roles of the troponin isoforms during indirect flight muscle development in Drosophila." Journal of Genetics 98, no. 5 (2019). http://dx.doi.org/10.1007/s12041-019-1150-x.

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