This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lees-Miller, J P
Right arrow Articles by Helfman, D M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lees-Miller, J P
Right arrow Articles by Helfman, D M

 Previous Article  |  Next Article 

Mol Cell Biol. 1990 April; 10(4): 1729-1742

Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing.

J P Lees-Miller, L O Goodwin and D M Helfman

Cold Spring Harbor Laboratory, New York 11724.

ABSTRACT

cDNA clones encoding three novel tropomyosins, termed TMBr-1, TMBr-2, and TMBr-3, were isolated and characterized from a rat brain cDNA library. All are derived from a single gene, which was previously found to express striated muscle alpha-tropomyosin and a number of other tropomyosin isoforms via an alternative splicing mechanism (N. Ruiz-Opazo and B. Nadal-Ginard, J. Biol. Chem. 262:4755-4765, 1987; D. F. Wieczorek, C. W. J. Smith, and B. Nadal-Ginard, Mol. Cell. Biol. 8:679-694, 1988). The derived amino acid sequences revealed that TMBr-1 contains 281 amino acids, TMBr-2 contains 251 amino acids, and TMBr-3 contains 245 amino acids. All three proteins contain a region that is identical to amino acids 81 through 258 of skeletal muscle alpha-tropomyosin. TMBr-1 is identical to striated muscle alpha-tropomyosin from amino acids 1 through 258 but contains a novel COOH-terminal region from amino acids 259 through 281. TMBr-2 and TMBr-3 both contain identical NH2-terminal sequences from amino acids 1 through 44 which were found to be expressed from a novel promoter. TMBr-3 contains the same COOH-terminal region as TMBr-1, whereas TMBr-2 contains a second novel COOH-terminal region. The genomic organization of the exons encoding TMBr-1, TMBr-2, and TMBr-3 were determined. These studies revealed a previously uncharacterized promoter located in the internal region of the alpha-TM gene as well as two novel COOH-terminal coding exons. The alpha-TM gene is a complex transcription unit containing 15 exons including two alternative promoters, two internal mutually exclusive exon cassettes, and four alternatively spliced 3' exons that encode four different COOH-terminal coding regions. A total of nine distinct mRNAs are known to be expressed from the alpha-TM gene in a cell type-specific manner in tissues such as striated muscle, smooth muscle, kidney, liver, brain, and fibroblasts. The mRNAs encoding TMBr-1, TMBr-2, and TMBr-3 were found to be expressed only in brain tissue, with TMBr-3 being expressed at much greater levels than TMBr-1 and TMBr-2. The individual structural characteristics of each brain alpha-tropomyosin isoform and their possible functions are discussed.

Mol Cell Biol. 1990 April; 10(4): 1729-1742




This article has been cited by other articles:

  • Anquetil, V., Le Sommer, C., Mereau, A., Hamon, S., Lerivray, H., Hardy, S. (2009). Polypyrimidine Tract Binding Protein Prevents Activity of an Intronic Regulatory Element That Promotes Usage of a Composite 3'-Terminal Exon. J. Biol. Chem. 284: 32370-32383 [Abstract] [Full Text]  
  • Schevzov, G., Fath, T., Vrhovski, B., Vlahovich, N., Rajan, S., Hook, J., Joya, J. E., Lemckert, F., Puttur, F., Lin, J. J.-C., Hardeman, E. C., Wieczorek, D. F., O'Neill, G. M., Gunning, P. W. (2008). Divergent Regulation of the Sarcomere and the Cytoskeleton. J. Biol. Chem. 283: 275-283 [Abstract] [Full Text]  
  • Gunning, P., O'neill, G., Hardeman, E. (2008). Tropomyosin-Based Regulation of the Actin Cytoskeleton in Time and Space. Physiol. Rev. 88: 1-35 [Abstract] [Full Text]  
  • Kubo, T., Wada, T., Yamaguchi, Y., Shimizu, A., Handa, H. (2006). Knock-down of 25 kDa subunit of cleavage factor Im in Hela cells alters alternative polyadenylation within 3'-UTRs. Nucleic Acids Res 34: 6264-6271 [Abstract] [Full Text]  
  • Ellis, P. D., Smith, C. W. J., Kemp, P. (2004). Regulated Tissue-specific Alternative Splicing of Enhanced Green Fluorescent Protein Transgenes Conferred by {alpha}-Tropomyosin Regulatory Elements in Transgenic Mice. J. Biol. Chem. 279: 36660-36669 [Abstract] [Full Text]  
  • Hamon, S., Le Sommer, C., Mereau, A., Allo, M.-R., Hardy, S. (2004). Polypyrimidine Tract-binding Protein Is Involved in Vivo in Repression of a Composite Internal/3' -Terminal Exon of the Xenopus {alpha}-Tropomyosin Pre-mRNA. J. Biol. Chem. 279: 22166-22175 [Abstract] [Full Text]  
  • Gaffin, R. D., Gokulan, K., Sacchettini, J. C., Hewett, T., Klevitsky, R., Robbins, J., Muthuchamy, M. (2004). Charged residue changes in the carboxy-terminus of {alpha}-tropomyosin alter mouse cardiac muscle contractility. J. Physiol. 556: 531-543 [Abstract] [Full Text]  
  • Janssen, R. A. J., Kim, P. N., Mier, J. W., Morrison, D. K. (2003). Overexpression of Kinase Suppressor of Ras Upregulates the High-Molecular-Weight Tropomyosin Isoforms in ras-Transformed NIH 3T3 Fibroblasts. Mol. Cell. Biol. 23: 1786-1797 [Abstract] [Full Text]  
  • Bryce, N. S., Schevzov, G., Ferguson, V., Percival, J. M., Lin, J. J.-C., Matsumura, F., Bamburg, J. R., Jeffrey, P. L., Hardeman, E. C., Gunning, P., Weinberger, R. P. (2003). Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms. Mol. Biol. Cell 14: 1002-1016 [Abstract] [Full Text]  
  • Guy, P. M., Kenny, D. A., Gill, G. N. (1999). The PDZ Domain of the LIM Protein Enigma Binds to beta -Tropomyosin. Mol. Biol. Cell 10: 1973-1984 [Abstract] [Full Text]  
  • Dufour, C., Weinberger, R. P., Schevzov, G., Jeffrey, P. L., Gunning, P. (1998). Splicing of Two Internal and Four Carboxyl-terminal Alternative Exons in Nonmuscle Tropomyosin 5 Pre-mRNA Is Independently Regulated during Development. J. Biol. Chem. 273: 18547-18555 [Abstract] [Full Text]  
  • Blanchard, E. M., Iizuka, K., Christe, M., Conner, D. A., Geisterfer-Lowrance, A., Schoen, F. J., Maughan, D. W., Seidman, C. E., Seidman, J.G. (1997). Targeted Ablation of the Murine {alpha}-Tropomyosin Gene. Circ. Res. 81: 1005-1010 [Abstract] [Full Text]  
  • James, J., Robbins, J. (1997). Molecular remodeling of cardiac contractile function. Am. J. Physiol. Heart Circ. Physiol. 273: H2105-H2118 [Abstract] [Full Text]  
  • Bastos, R., Pouplana, L. R. d., Enarson, M., Bodoor, K., Burke, B. (1997). Nup84, A Novel Nucleoporin That Is Associated With CAN/Nup214 on the Cytoplasmic Face of the Nuclear Pore Complex. JCB 137: 989-1000 [Abstract] [Full Text]  
  • Hammell, R. L., Hitchcock-DeGregori, S. E. (1996). Mapping the Functional Domains within the Carboxyl Terminus of alpha-Tropomyosin Encoded by the Alternatively Spliced Ninth Exon. J. Biol. Chem. 271: 4236-4242 [Abstract] [Full Text]  
  • Watakabe, A, Kobayashi, R, Helfman, D. (1996). N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin. J. Cell Sci. 109: 2299-2310 [Abstract]  
  • Pittenger, M., Kistler, A, Helfman, D. (1995). Alternatively spliced exons of the beta tropomyosin gene exhibit different affinities for F-actin and effects with nonmuscle caldesmon. J. Cell Sci. 108: 3253-3265 [Abstract]  
  • Had, L, Faivre-Sarrailh, C, Legrand, C, Mery, J, Brugidou, J, Rabie, A (1994). Tropomyosin isoforms in rat neurons: the different developmental profiles and distributions of TM-4 and TMBr-3 are consistent with different functions. J. Cell Sci. 107: 2961-2973 [Abstract]  
  • Mullen, M P, Smith, C W, Patton, J G, Nadal-Ginard, B (1991). Alpha-tropomyosin mutually exclusive exon selection: competition between branchpoint/polypyrimidine tracts determines default exon choice.. Genes Dev. 5: 642-655 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»