Complete nucleotide sequence of a soybean actin gene.
PDF (976K)
Journal: 2010/June - Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
PUBMED: 16593157
Abstract:
Soybean contains a small multigene family of actin-related sequences. We have determined the complete nucleotide sequence of a soybean actin gene carried on the recombinant plasmid pSAc3. As deduced from the nucleotide sequence, this soybean actin is composed of 376 amino acids. Compared to other eukaryotic actins, pSAc3 actin has a deletion of one amino acid between residues 118 and 122. The initiator methionine is followed by alanine, which is not found at this position in other eukaryotic actins. pSAc3 actin differs, in primary sequence, more from fungal and animal actins than any of the known nonplant actins differ from each other. pSAc3 actin appears to be related to both cytoplasmic and muscle specific actins in the location of specific NH(2)-terminal amino acids. The coding sequence is interrupted by three small introns, each less than 90 base pairs long. The splice junctions are similar to those found in other eukaryotic genes, suggesting the presence of a similar splicing apparatus in higher plants. Introns 1 and 3 interrupt the reading frame after codons 20 and 355, respectively. Intron 2 splits a glycine codon at position 151. None of these intron positions is conserved relative to the positions of introns in other actin genes examined.
Open in
PUBMED | PMC | Google Scholar | Wikipedia
Relations:
Content
Citations
(87)
References
(27)
Drugs
(1)
Genes
(1)
Affiliates
(1)
Similar articles
Articles by the same authors
Discussion board
Proc Natl Acad Sci U S A 79(4): 1022-1026
PMID: 16593157

Complete nucleotide sequence of a soybean actin gene

Abstract

Soybean contains a small multigene family of actin-related sequences. We have determined the complete nucleotide sequence of a soybean actin gene carried on the recombinant plasmid pSAc3. As deduced from the nucleotide sequence, this soybean actin is composed of 376 amino acids. Compared to other eukaryotic actins, pSAc3 actin has a deletion of one amino acid between residues 118 and 122. The initiator methionine is followed by alanine, which is not found at this position in other eukaryotic actins. pSAc3 actin differs, in primary sequence, more from fungal and animal actins than any of the known nonplant actins differ from each other. pSAc3 actin appears to be related to both cytoplasmic and muscle specific actins in the location of specific NH2-terminal amino acids. The coding sequence is interrupted by three small introns, each less than 90 base pairs long. The splice junctions are similar to those found in other eukaryotic genes, suggesting the presence of a similar splicing apparatus in higher plants. Introns 1 and 3 interrupt the reading frame after codons 20 and 355, respectively. Intron 2 splits a glycine codon at position 151. None of these intron positions is conserved relative to the positions of introns in other actin genes examined.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (976K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
icon of scanned page 1022
1022
icon of scanned page 1023
1023
icon of scanned page 1024
1024
icon of scanned page 1025
1025
icon of scanned page 1026
1026

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Kersey YM, Hepler PK, Palevitz BA, Wessells NK. Polarity of actin filaments in Characean algae. Proc Natl Acad Sci U S A. 1976 Jan;73(1):165–167.[PMC free article] [PubMed] [Google Scholar]
  • Kersey YM, Wessells NK. Localization of actin filaments in internodal cells of characean algae. A scanning and transmission electron microscope study. J Cell Biol. 1976 Feb;68(2):264–275.[PMC free article] [PubMed] [Google Scholar]
  • Vandekerckhove J, Weber K. The amino acid sequence of Physarum actin. Nature. 1978 Dec 14;276(5689):720–721. [PubMed] [Google Scholar]
  • Vandekerckhove J, Weber K. At least six different actins are expressed in a higher mammal: an analysis based on the amino acid sequence of the amino-terminal tryptic peptide. J Mol Biol. 1978 Dec 25;126(4):783–802. [PubMed] [Google Scholar]
  • Gallwitz D, Seidel R. Molecular cloning of the actin gene from yeast Saccharomyces cerevisiae. Nucleic Acids Res. 1980 Mar 11;8(5):1043–1059.[PMC free article] [PubMed] [Google Scholar]
  • Gallwitz D, Sures I. Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 May;77(5):2546–2550.[PMC free article] [PubMed] [Google Scholar]
  • Ng R, Abelson J. Isolation and sequence of the gene for actin in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 Jul;77(7):3912–3916.[PMC free article] [PubMed] [Google Scholar]
  • Vandekerckhove J, Weber K. Vegetative Dictyostelium cells containing 17 actin genes express a single major actin. Nature. 1980 Apr 3;284(5755):475–477. [PubMed] [Google Scholar]
  • Fyrberg EA, Bond BJ, Hershey ND, Mixter KS, 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. [PubMed] [Google Scholar]
  • Nagao RT, Shah DM, Eckenrode VK, Meagher RB. Multigene family of actin-related sequences isolated from a soybean genomic library. DNA. 1981;1(1):1–9. [PubMed] [Google Scholar]
  • Meagher RB, Shepherd RJ, Boyer HW. The structure of cauliflower mosaic virus. I. A restriction endonuclease map of cauliflower mosaic virus DNA. Virology. 1977 Jul 15;80(2):362–375. [PubMed] [Google Scholar]
  • Yang R, Lis J, Wu R. Elution of DNA from agarose gels after electrophoresis. Methods Enzymol. 1979;68:176–182. [PubMed] [Google Scholar]
  • Carreira LH, Carlton BC, Bobbio SM, Nagao RT, Meagher RB. Construction and application of a modified "gene machine": a circular concentrating preparative gel electrophoresis device employing discontinuous elution. Anal Biochem. 1980 Aug;106(2):455–468. [PubMed] [Google Scholar]
  • Smith HO, Birnstiel ML. A simple method for DNA restriction site mapping. Nucleic Acids Res. 1976 Sep;3(9):2387–2398.[PMC free article] [PubMed] [Google Scholar]
  • Maxam AM, Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. [PubMed] [Google Scholar]
  • Lerner MR, Boyle JA, Mount SM, Wolin SL, Steitz JA. Are snRNPs involved in splicing? Nature. 1980 Jan 10;283(5743):220–224. [PubMed] [Google Scholar]
  • Baralle FE, Shoulders CC, Proudfoot NJ. The primary structure of the human epsilon-globin gene. Cell. 1980 Oct;21(3):621–626. [PubMed] [Google Scholar]
  • Efstratiadis A, Posakony JW, Maniatis T, Lawn RM, O'Connell C, Spritz RA, DeRiel JK, Forget BG, Weissman SM, Slightom JL, et al. The structure and evolution of the human beta-globin gene family. Cell. 1980 Oct;21(3):653–668. [PubMed] [Google Scholar]
  • Sakano H, Rogers JH, Hüppi K, Brack C, Traunecker A, Maki R, Wall R, Tonegawa S. Domains and the hinge region of an immunoglobulin heavy chain are encoded in separate DNA segments. Nature. 1979 Feb 22;277(5698):627–633. [PubMed] [Google Scholar]
  • Stein JP, Catterall JF, Kristo P, Means AR, O'Malley BW. Ovomucoid intervening sequences specify functional domains and generate protein polymorphism. Cell. 1980 Oct;21(3):681–687. [PubMed] [Google Scholar]
  • Durica DS, Schloss JA, Crain WR., Jr Organization of actin gene sequences in the sea urchin: molecular cloning of an intron-containing DNA sequence coding for a cytoplasmic actin. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5683–5687.[PMC free article] [PubMed] [Google Scholar]
  • Firtel RA. Multigene families encoding actin and tubulin. Cell. 1981 Apr;24(1):6–7. [PubMed] [Google Scholar]
  • Gilbert W. Why genes in pieces? Nature. 1978 Feb 9;271(5645):501–501. [PubMed] [Google Scholar]
  • Go M. Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature. 1981 May 7;291(5810):90–92. [PubMed] [Google Scholar]
  • Tonegawa S, Maxam AM, Tizard R, Bernard O, Gilbert W. Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1485–1489.[PMC free article] [PubMed] [Google Scholar]
  • Gallwitz D, Perrin F, Seidel R. The actin gene in yeast Saccharomyces cerevisiae: 5' and 3' end mapping, flanking and putative regulatory sequences. Nucleic Acids Res. 1981 Dec 11;9(23):6339–6350.[PMC free article] [PubMed] [Google Scholar]
  • Hentschel C, Irminger JC, Bucher P, Birnstiel ML. Sea urchin histone mRNA termini are located in gene regions downstream from putative regulatory sequences. Nature. 1980 May 15;285(5761):147–151. [PubMed] [Google Scholar]
Department of Molecular and Population Genetics, University of Georgia, Athens, Georgia 30602
Copyright notice
Abstract
Soybean contains a small multigene family of actin-related sequences. We have determined the complete nucleotide sequence of a soybean actin gene carried on the recombinant plasmid pSAc3. As deduced from the nucleotide sequence, this soybean actin is composed of 376 amino acids. Compared to other eukaryotic actins, pSAc3 actin has a deletion of one amino acid between residues 118 and 122. The initiator methionine is followed by alanine, which is not found at this position in other eukaryotic actins. pSAc3 actin differs, in primary sequence, more from fungal and animal actins than any of the known nonplant actins differ from each other. pSAc3 actin appears to be related to both cytoplasmic and muscle specific actins in the location of specific NH2-terminal amino acids. The coding sequence is interrupted by three small introns, each less than 90 base pairs long. The splice junctions are similar to those found in other eukaryotic genes, suggesting the presence of a similar splicing apparatus in higher plants. Introns 1 and 3 interrupt the reading frame after codons 20 and 355, respectively. Intron 2 splits a glycine codon at position 151. None of these intron positions is conserved relative to the positions of introns in other actin genes examined.
Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.