Abstract
Four cDNA clones coding for different Artemia actin isoforms have been isolated. Three of the clones contain the complete coding sequences while the fourth one lacks 145 bases, coding for the 49 amino terminal amino acids of the protein. The amino acid sequences predicted for the four actin isoforms identified are highly homologous to insect actins as well as to vertebrate cytoplasmic actins. The four identified cDNA clones code for mRNAs of 5.2, 1.9, 1.6 and 1.8 kb, respectively, whose expression is regulated during development. Three of the actin mRNAs are present in cryptobiotic embryos while the other is not. The steady-state levels of all four mRNAs increase during development to reach maximal levels by 10-15 hours of development and decrease thereafter. The total number of actin genes encoded in the Artemia genome has been estimated as 8 to 10 by Southern analysis of total DNA.
Full text
PDF






Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Adams S. L., Sobel M. E., Howard B. H., Olden K., Yamada K. M., de Crombrugghe B., Pastan I. Levels of translatable mRNAs for cell surface protein, collagen precursors, and two membrane proteins are altered in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3399–3403. doi: 10.1073/pnas.74.8.3399. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Akhurst R. J., Calzone F. J., Lee J. J., Britten R. J., Davidson E. H. Structure and organization of the CyIII actin gene subfamily of the sea urchin, Strongylocentrotus purpuratus. J Mol Biol. 1987 Mar 20;194(2):193–203. doi: 10.1016/0022-2836(87)90368-8. [DOI] [PubMed] [Google Scholar]
- Benton W. D., Davis R. W. Screening lambdagt recombinant clones by hybridization to single plaques in situ. Science. 1977 Apr 8;196(4286):180–182. doi: 10.1126/science.322279. [DOI] [PubMed] [Google Scholar]
- Carroll S. L., Bergsma D. J., Schwartz R. J. A 29-nucleotide DNA segment containing an evolutionarily conserved motif is required in cis for cell-type-restricted repression of the chicken alpha-smooth muscle actin gene core promoter. Mol Cell Biol. 1988 Jan;8(1):241–250. doi: 10.1128/mcb.8.1.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chen E. Y., Seeburg P. H. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA. 1985 Apr;4(2):165–170. doi: 10.1089/dna.1985.4.165. [DOI] [PubMed] [Google Scholar]
- Cruces J., Sebastián J., Renart J. Restriction mapping of the rRNA genes from Artemia larvae. Biochem Biophys Res Commun. 1981 Jan 30;98(2):404–409. doi: 10.1016/0006-291x(81)90854-8. [DOI] [PubMed] [Google Scholar]
- Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
- Field K. G., Olsen G. J., Lane D. J., Giovannoni S. J., Ghiselin M. T., Raff E. C., Pace N. R., Raff R. A. Molecular phylogeny of the animal kingdom. Science. 1988 Feb 12;239(4841 Pt 1):748–753. doi: 10.1126/science.3277277. [DOI] [PubMed] [Google Scholar]
- Fyrberg E. A., Bond B. J., Hershey N. D., Mixter K. S., Davidson N. The actin genes of Drosophila: protein coding regions are highly conserved but intron positions are not. Cell. 1981 Apr;24(1):107–116. doi: 10.1016/0092-8674(81)90506-7. [DOI] [PubMed] [Google Scholar]
- Fyrberg E. A., Kindle K. L., Davidson N., Kindle K. L. The actin genes of Drosophila: a dispersed multigene family. Cell. 1980 Feb;19(2):365–378. doi: 10.1016/0092-8674(80)90511-5. [DOI] [PubMed] [Google Scholar]
- Fyrberg E. A., Mahaffey J. W., Bond B. J., Davidson N. Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Cell. 1983 May;33(1):115–123. doi: 10.1016/0092-8674(83)90340-9. [DOI] [PubMed] [Google Scholar]
- Goodman M., Pedwaydon J., Czelusniak J., Suzuki T., Gotoh T., Moens L., Shishikura F., Walz D., Vinogradov S. An evolutionary tree for invertebrate globin sequences. J Mol Evol. 1988;27(3):236–249. doi: 10.1007/BF02100080. [DOI] [PubMed] [Google Scholar]
- Guo L. H., Yang R. C., Wu R. An improved strategy for rapid direct sequencing of both strands of long DNA molecules cloned in a plasmid. Nucleic Acids Res. 1983 Aug 25;11(16):5521–5540. doi: 10.1093/nar/11.16.5521. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hanahan D., Meselson M. Plasmid screening at high colony density. Gene. 1980 Jun;10(1):63–67. doi: 10.1016/0378-1119(80)90144-4. [DOI] [PubMed] [Google Scholar]
- Hough-Evans B. R., Franks R. R., Cameron R. A., Britten R. J., Davidson E. H. Correct cell-type-specific expression of a fusion gene injected into sea urchin eggs. Dev Biol. 1987 Jun;121(2):576–579. doi: 10.1016/0012-1606(87)90193-x. [DOI] [PubMed] [Google Scholar]
- Johnson P. J., Foran D. R., Moore G. P. Organization and evolution of the actin gene family in sea urchins. Mol Cell Biol. 1983 Oct;3(10):1824–1833. doi: 10.1128/mcb.3.10.1824. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Koller H. T., Frondorf K. A., Maschner P. D., Vaughn J. C. In vivo transcription from multiple spacer rRNA gene promoters during early development and evolution of the intergenic spacer in the brine shrimp Artemia. Nucleic Acids Res. 1987 Jul 10;15(13):5391–5411. doi: 10.1093/nar/15.13.5391. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
- McKeown M., Firtel R. A. Evidence for sub-families of actin genes in Dictyostelium as determined by comparisons of 3' end sequences. J Mol Biol. 1981 Oct 5;151(4):593–606. doi: 10.1016/0022-2836(81)90425-3. [DOI] [PubMed] [Google Scholar]
- McKeown M., Taylor W. C., Kindle K. L., Firtel R. A., Bender W., Davidson N. Multiple, heterogeneous actin genes in Dictyostelium. Cell. 1978 Nov;15(3):789–800. doi: 10.1016/0092-8674(78)90264-7. [DOI] [PubMed] [Google Scholar]
- Minty A., Kedes L. Upstream regions of the human cardiac actin gene that modulate its transcription in muscle cells: presence of an evolutionarily conserved repeated motif. Mol Cell Biol. 1986 Jun;6(6):2125–2136. doi: 10.1128/mcb.6.6.2125. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miwa T., Kedes L. Duplicated CArG box domains have positive and mutually dependent regulatory roles in expression of the human alpha-cardiac actin gene. Mol Cell Biol. 1987 Aug;7(8):2803–2813. doi: 10.1128/mcb.7.8.2803. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mohun T. J., Brennan S., Dathan N., Fairman S., Gurdon J. B. Cell type-specific activation of actin genes in the early amphibian embryo. Nature. 1984 Oct 25;311(5988):716–721. doi: 10.1038/311716a0. [DOI] [PubMed] [Google Scholar]
- Mohun T. J., Taylor M. V., Garrett N., Gurdon J. B. The CArG promoter sequence is necessary for muscle-specific transcription of the cardiac actin gene in Xenopus embryos. EMBO J. 1989 Apr;8(4):1153–1161. doi: 10.1002/j.1460-2075.1989.tb03486.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Osuna C., Sebastián J. Levels of the RNA polymerases during the early larval development of Artemia. Eur J Biochem. 1980 Aug;109(2):383–389. doi: 10.1111/j.1432-1033.1980.tb04805.x. [DOI] [PubMed] [Google Scholar]
- Palmero I., Renart J., Sastre L. Isolation of cDNA clones coding for mitochondrial 16S ribosomal RNA from the crustacean Artemia. Gene. 1988 Sep 7;68(2):239–248. doi: 10.1016/0378-1119(88)90026-1. [DOI] [PubMed] [Google Scholar]
- Palmero I., Sastre L. Complementary DNA cloning of a protein highly homologous to mammalian sarcoplasmic reticulum Ca-ATPase from the crustacean Artemia. J Mol Biol. 1989 Dec 20;210(4):737–748. doi: 10.1016/0022-2836(89)90106-x. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Cooper J. A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem. 1986;55:987–1035. doi: 10.1146/annurev.bi.55.070186.005011. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
- Reed K. C., Mann D. A. Rapid transfer of DNA from agarose gels to nylon membranes. Nucleic Acids Res. 1985 Oct 25;13(20):7207–7221. doi: 10.1093/nar/13.20.7207. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sanchez F., Tobin S. L., Rdest U., Zulauf E., McCarthy B. J. Two Drosophila actin genes in detail. Gene structure, protein structure and transcription during development. J Mol Biol. 1983 Feb 5;163(4):533–551. doi: 10.1016/0022-2836(83)90111-0. [DOI] [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scheller R. H., McAllister L. B., Crain W. R., Jr, Durica D. S., Posakony J. W., Thomas T. L., Britten R. J., Davidson E. H. Organization and expression of multiple actin genes in the sea urchin. Mol Cell Biol. 1981 Jul;1(7):609–628. doi: 10.1128/mcb.1.7.609. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shott R. J., Lee J. J., Britten R. J., Davidson E. H. Differential expression of the actin gene family of Strongylocentrotus purpuratus. Dev Biol. 1984 Feb;101(2):295–306. doi: 10.1016/0012-1606(84)90143-x. [DOI] [PubMed] [Google Scholar]
- Solomon L. R., Rubenstein P. A. Correct NH2-terminal processing of cardiac muscle alpha-isoactin (class II) in a nonmuscle mouse cell. J Biol Chem. 1985 Jun 25;260(12):7659–7664. [PubMed] [Google Scholar]
- Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tobin S. L., Zulauf E., Sánchez F., Craig E. A., McCarthy B. J. Multiple actin-related sequences in the Drosophila melanogaster genome. Cell. 1980 Jan;19(1):121–131. doi: 10.1016/0092-8674(80)90393-1. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J., Franke W. W., Weber K. Diversity of expression of non-muscle actin in amphibia. J Mol Biol. 1981 Oct 25;152(2):413–426. doi: 10.1016/0022-2836(81)90251-5. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J., Weber K. Chordate muscle actins differ distinctly from invertebrate muscle actins. The evolution of the different vertebrate muscle actins. J Mol Biol. 1984 Nov 5;179(3):391–413. doi: 10.1016/0022-2836(84)90072-x. [DOI] [PubMed] [Google Scholar]
- Volk T., Geiger B., Raz A. Motility and adhesive properties of high- and low-metastatic murine neoplastic cells. Cancer Res. 1984 Feb;44(2):811–824. [PubMed] [Google Scholar]
- Woods D. E., Markham A. F., Ricker A. T., Goldberger G., Colten H. R. Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product. Proc Natl Acad Sci U S A. 1982 Sep;79(18):5661–5665. doi: 10.1073/pnas.79.18.5661. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]