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. 1983 Oct;3(10):1783–1791. doi: 10.1128/mcb.3.10.1783

Human actin genes are single copy for alpha-skeletal and alpha-cardiac actin but multicopy for beta- and gamma-cytoskeletal genes: 3' untranslated regions are isotype specific but are conserved in evolution.

P Ponte, P Gunning, H Blau, L Kedes
PMCID: PMC370040  PMID: 6646124

Abstract

We have constructed isotype-specific subclones from the 3' untranslated regions of alpha-skeletal, alpha-cardiac, beta-cytoskeletal, and gamma-cytoskeletal actin cDNAs. These clones have been used as hybridization probes to assay the number and organization of these actin isotypes in the human genome. Hybridization of these probes to human genomic actin clones (Engel et al., Proc. Natl. Acad. Sci. U.S.A. 78:4674-4678, 1981; Engel et al., Mol. Cell. Biol. 2:674-684, 1982) has allowed the unambiguous assignment of the genomic clones to isotypically defined actin subfamilies. In addition, only one isotype-specific probe hybridizes to each actin-containing gene, with a single exception. This result suggests that the multiple actin genes in the human genome are not closely linked. Genomic DNA blots probed with these subclones under stringent conditions demonstrate that the alpha-skeletal and alpha-cardiac muscle actin genes are single copy, whereas the cytoskeletal actins, beta and gamma, are present in multiple copies in the human genome. Most of the actin genes of other mammals are cytoplasmic as well. These observations have important implications for the evolution of multigene families.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alwine J. C., Kemp D. J., Stark G. R. Method for detection of specific RNAs in agarose gels by transfer to diazobenzyloxymethyl-paper and hybridization with DNA probes. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5350–5354. doi: 10.1073/pnas.74.12.5350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baltimore D. Gene conversion: some implications for immunoglobulin genes. Cell. 1981 Jun;24(3):592–594. doi: 10.1016/0092-8674(81)90082-9. [DOI] [PubMed] [Google Scholar]
  3. Blau H. M., Webster C. Isolation and characterization of human muscle cells. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5623–5627. doi: 10.1073/pnas.78.9.5623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brawerman G., Mendecki J., Lee S. Y. A procedure for the isolation of mammalian messenger ribonucleic acid. Biochemistry. 1972 Feb 15;11(4):637–641. doi: 10.1021/bi00754a027. [DOI] [PubMed] [Google Scholar]
  5. Childs G., Maxson R., Kedes L. H. Histone gene expression during sea urchin embryogenesis: isolation and characterization of early and late messenger RNAs of Strongylocentrotus purpuratus by gene-specific hybridization and template activity. Dev Biol. 1979 Nov;73(1):153–173. doi: 10.1016/0012-1606(79)90144-1. [DOI] [PubMed] [Google Scholar]
  6. Cleveland D. W., Lopata M. A., MacDonald R. J., Cowan N. J., Rutter W. J., Kirschner M. W. Number and evolutionary conservation of alpha- and beta-tubulin and cytoplasmic beta- and gamma-actin genes using specific cloned cDNA probes. Cell. 1980 May;20(1):95–105. doi: 10.1016/0092-8674(80)90238-x. [DOI] [PubMed] [Google Scholar]
  7. Engel J. N., Gunning P. W., Kedes L. Isolation and characterization of human actin genes. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4674–4678. doi: 10.1073/pnas.78.8.4674. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Engel J., Gunning P., Kedes L. Human cytoplasmic actin proteins are encoded by a multigene family. Mol Cell Biol. 1982 Jun;2(6):674–684. doi: 10.1128/mcb.2.6.674. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gunning P., Ponte P., Okayama H., Engel J., Blau H., Kedes L. Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed. Mol Cell Biol. 1983 May;3(5):787–795. doi: 10.1128/mcb.3.5.787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hamada H., Petrino M. G., Kakunaga T. Molecular structure and evolutionary origin of human cardiac muscle actin gene. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5901–5905. doi: 10.1073/pnas.79.19.5901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hanukoglu I., Tanese N., Fuchs E. Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions. J Mol Biol. 1983 Feb 5;163(4):673–678. doi: 10.1016/0022-2836(83)90117-1. [DOI] [PubMed] [Google Scholar]
  12. Lee M. G., Lewis S. A., Wilde C. D., Cowan N. J. Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes. Cell. 1983 Jun;33(2):477–487. doi: 10.1016/0092-8674(83)90429-4. [DOI] [PubMed] [Google Scholar]
  13. McKeown M., Firtel R. A. Differential expression and 5' end mapping of actin genes in Dictyostelium. Cell. 1981 Jun;24(3):799–807. doi: 10.1016/0092-8674(81)90105-7. [DOI] [PubMed] [Google Scholar]
  14. McMaster G. K., Carmichael G. G. Analysis of single- and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4835–4838. doi: 10.1073/pnas.74.11.4835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Minty A. J., Alonso S., Guénet J. L., Buckingham M. E. Number and organization of actin-related sequences in the mouse genome. J Mol Biol. 1983 Jun 15;167(1):77–101. doi: 10.1016/s0022-2836(83)80035-7. [DOI] [PubMed] [Google Scholar]
  16. Moos M., Gallwitz D. Structure of a human beta-actin-related pseudogene which lacks intervening sequences. Nucleic Acids Res. 1982 Dec 11;10(23):7843–7849. doi: 10.1093/nar/10.23.7843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Moos M., Gallwitz D. Structure of two human beta-actin-related processed genes one of which is located next to a simple repetitive sequence. EMBO J. 1983;2(5):757–761. doi: 10.1002/j.1460-2075.1983.tb01496.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Nudel U., Katcoff D., Zakut R., Shani M., Carmon Y., Finer M., Czosnek H., Ginsburg I., Yaffe D. Isolation and characterization of rat skeletal muscle and cytoplasmic actin genes. Proc Natl Acad Sci U S A. 1982 May;79(9):2763–2767. doi: 10.1073/pnas.79.9.2763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ponte P. A., Siekevitz M., Schwartz R. C., Gefter M. L., Sonenshein G. E. Transcription of immunoglobulin heavy-chain sequences from the excluded allele. Nature. 1981 Jun 18;291(5816):594–596. doi: 10.1038/291594a0. [DOI] [PubMed] [Google Scholar]
  20. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  21. Scarpulla R. C., Wu R. Nonallelic members of the cytochrome c multigene family of the rat may arise through different messenger RNAs. Cell. 1983 Feb;32(2):473–482. doi: 10.1016/0092-8674(83)90467-1. [DOI] [PubMed] [Google Scholar]
  22. Vandekerckhove J., Weber K. Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1106–1110. doi: 10.1073/pnas.75.3.1106. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Vandekerckhove J., Weber K. The amino acid sequence of actin from chicken skeletal muscle actin and chicken gizzard smooth muscle actin. FEBS Lett. 1979 Jun 15;102(2):219–222. doi: 10.1016/0014-5793(79)80004-6. [DOI] [PubMed] [Google Scholar]
  24. Vandekerckhove J., Weber K. The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation. Differentiation. 1979;14(3):123–133. doi: 10.1111/j.1432-0436.1979.tb01021.x. [DOI] [PubMed] [Google Scholar]

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