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Molecular and Cellular Biology, March 2004, p. 2318-2323, Vol. 24, No. 6
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.6.2318-2323.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Gamma Tropomyosin Gene Products Are Required for Embryonic Development

J. Hook,1 F. Lemckert,1 H. Qin,2 G. Schevzov,1,3 and P. Gunning1,3*

Oncology Research Unit, The Children's Hospital at Westmead, Westmead, New South Wales 2145,1 Discipline of Paediatrics and Child Health, The University of Sydney, Sydney, New South Wales 2006,3 Douglas Hanley Moir Laboratories, North Ryde, New South Wales 2113, Australia2

Received 26 August 2003/ Accepted 12 November 2003

The actin filament system is essential for many cellular functions, including shape, motility, cytokinesis, intracellular trafficking, and tissue organization. Tropomyosins (Tms) are rod-like components of most actin filaments that differentially affect their stability and flexibility. The Tm gene family consists of four genes, {alpha}Tm, ßTm, {gamma}Tm (Tm5 NM, where "NM" indicates "nonmuscle"), and {delta}Tm (Tm4). Multiple isoforms of the Tm family are generated by alternative splicing of three of these genes, and their expression is highly regulated. Extensive spatial and temporal sorting of Tm isoforms into different cellular compartments has been shown to occur in several cell types. We have addressed the function of the low-molecular-weight Tms encoded by the {gamma}Tm gene by eliminating the corresponding amino-terminal coding sequences from this gene. Heterozygous mice were generated, and subsequent intercrossing of the F1 pups did not result in any viable homozygous knockouts. Genotype analysis of day 2.5 morulae also failed to detect any homozygous knockouts. We have failed in our attempts to delete the second allele and generate in vitro double-knockout cells, although 51 clones displayed homologous recombination back into the originally targeted locus. We therefore conclude that low-molecular-weight products from the {gamma}Tm gene are essential for both embryonic development and cell survival.

* Corresponding author. Mailing address: Oncology Research Unit, Clinical Sciences Building, The Children's Hospital at Westmead, 216 Hawkesbury Rd., Westmead, NSW 2145, Australia. Phone: (61 2) 9845 3045. Fax: (61 2) 9845 3082. E-mail: PeterG3{at}chw.edu.au.

Molecular and Cellular Biology, March 2004, p. 2318-2323, Vol. 24, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.6.2318-2323.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Pasquet, S., Naye, F., Faucheux, C., Bronchain, O., Chesneau, A., Thiebaud, P., Theze, N. (2006). Transcription Enhancer Factor-1-dependent Expression of the {alpha}-Tropomyosin Gene in the Three Muscle Cell Types. J. Biol. Chem. 281: 34406-34420 [Abstract] [Full Text]  
  • Schevzov, G., Vrhovski, B., Bryce, N. S., Elmir, S., Qiu, M. R., O'Neill, G. M., Yang, N., Verrills, N. M., Kavallaris, M., Gunning, P. W. (2005). Tissue-specific Tropomyosin Isoform Composition. J. Histochem. Cytochem. 53: 557-570 [Abstract] [Full Text]  
  • Kee, A. J., Schevzov, G., Nair-Shalliker, V., Robinson, C. S., Vrhovski, B., Ghoddusi, M., Qiu, M. R., Lin, J. J.-C., Weinberger, R., Gunning, P. W., Hardeman, E. C. (2004). Sorting of a nonmuscle tropomyosin to a novel cytoskeletal compartment in skeletal muscle results in muscular dystrophy. JCB 166: 685-696 [Abstract] [Full Text]  


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