Abstract
Histone H2A is a component of eukaryotic chromatin whose expression has not been studied in plants. We isolated and characterized a tomato and a pea cDNA encoding histone H2A. We found that in tomato H2A is encoded by a small gene family and that both the pea and the tomato mRNAs are polyadenylated. Tomato H2A has 82% amino acid residue identity to pea H2A, 83% to wheat, and 65% to human and yeast H2A. Plant H2As differ from fungal and animal H2As in their amino-terminal and carboxy-terminal regions. Carboxy-terminal plant H2A regions contain the motif SPKK, a peptide implicated in binding of A/T-rich DNA regions. By using RNA gel blot analysis, we determined that the steady-state mRNA level of these genes was abundant in apices and early developing fruit and very low in mature tissues. In situ RNA hybridization showed strong spatial regulation because the mRNA was abundant in some cells and not detectable in others. In tomato shoot tips, H2A-expressing cells were distributed irregularly in or near meristems. In tomato or pea root tips, expressing cells were concentrated near the apex, and their distribution was consistent with that expected of cycling cells. Other H2A transcripts were found in nondividing cortical cells that are known to undergo endoduplication during the late maturation phase of primary development.
Full Text
The Full Text of this article is available as a PDF (3.3 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Alexander D. C. An efficient vector-primer cDNA cloning system. Methods Enzymol. 1987;154:41–64. doi: 10.1016/0076-6879(87)54069-1. [DOI] [PubMed] [Google Scholar]
- Chaboute M. E., Chaubet N., Clement B., Gigot C., Philipps G. Polyadenylation of histone H3 and H4 mRNAs in dicotyledonous plants. Gene. 1988 Nov 15;71(1):217–223. doi: 10.1016/0378-1119(88)90095-9. [DOI] [PubMed] [Google Scholar]
- Chaubet N., Chaboute M. E., Clément B., Ehling M., Philipps G., Gigot C. The histone H3 and H4 mRNAs are polyadenylated in maize. Nucleic Acids Res. 1988 Feb 25;16(4):1295–1304. doi: 10.1093/nar/16.4.1295. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Choe J., Kolodrubetz D., Grunstein M. The two yeast histone H2A genes encode similar protein subtypes. Proc Natl Acad Sci U S A. 1982 Mar;79(5):1484–1487. doi: 10.1073/pnas.79.5.1484. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Churchill M. E., Suzuki M. 'SPKK' motifs prefer to bind to DNA at A/T-rich sites. EMBO J. 1989 Dec 20;8(13):4189–4195. doi: 10.1002/j.1460-2075.1989.tb08604.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Colbert J. T., Hershey H. P., Quail P. H. Autoregulatory control of translatable phytochrome mRNA levels. Proc Natl Acad Sci U S A. 1983 Apr;80(8):2248–2252. doi: 10.1073/pnas.80.8.2248. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
- Hayashi T., Ohe Y., Hayashi H., Iwai K. Human spleen histone H2A. Isolation and four variant sequences. J Biochem. 1980 Jul;88(1):27–34. [PubMed] [Google Scholar]
- Marzluff W. F., Pandey N. B. Multiple regulatory steps control histone mRNA concentrations. Trends Biochem Sci. 1988 Feb;13(2):49–52. doi: 10.1016/0968-0004(88)90027-8. [DOI] [PubMed] [Google Scholar]
- Old R. W., Woodland H. R. Histone genes: not so simple after all. Cell. 1984 Oct;38(3):624–626. doi: 10.1016/0092-8674(84)90256-3. [DOI] [PubMed] [Google Scholar]
- Raghavan V., Olmedilla A. Spatial patterns of histone mRNA expression during grain development and germination in rice. Cell Differ Dev. 1989 Sep;27(3):183–196. doi: 10.1016/0922-3371(89)90699-0. [DOI] [PubMed] [Google Scholar]
- Schümperli D. Cell-cycle regulation of histone gene expression. Cell. 1986 May 23;45(4):471–472. doi: 10.1016/0092-8674(86)90277-1. [DOI] [PubMed] [Google Scholar]
- Sussex I. M. Developmental programming of the shoot meristem. Cell. 1989 Jan 27;56(2):225–229. doi: 10.1016/0092-8674(89)90895-7. [DOI] [PubMed] [Google Scholar]
- Tabata T., Sasaki K., Iwabuchi M. The structural organization and DNA sequence of a wheat histone H4 gene. Nucleic Acids Res. 1983 Sep 10;11(17):5865–5875. doi: 10.1093/nar/11.17.5865. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Taub F., Thompson E. B. An improved method for preparing large arrays of bacterial colonies containing plasmids for hybridization: in situ purification and stable binding of DNA on paper filters. Anal Biochem. 1982 Oct;126(1):222–230. doi: 10.1016/0003-2697(82)90133-6. [DOI] [PubMed] [Google Scholar]
- Thomas G., Padayatty J. D. Organization and bidirectional transcription of H2A, H2B and H4 histone genes in rice embryos. Nature. 1983 Nov 3;306(5938):82–84. doi: 10.1038/306082a0. [DOI] [PubMed] [Google Scholar]
- Wells D., McBride C. A comprehensive compilation and alignment of histones and histone genes. Nucleic Acids Res. 1989;17 (Suppl):r311–r346. doi: 10.1093/nar/17.suppl.r311. [DOI] [PMC free article] [PubMed] [Google Scholar]
- White E. M., Gorovsky M. A. Localization and expression of mRNA for a macronuclear-specific histone H2A variant (hv1) during the cell cycle and conjugation of Tetrahymena thermophila. Mol Cell Biol. 1988 Nov;8(11):4780–4786. doi: 10.1128/mcb.8.11.4780. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wu S. C., Györgyey J., Dudits D. Polyadenylated H3 histone transcripts and H3 histone variants in alfalfa. Nucleic Acids Res. 1989 Apr 25;17(8):3057–3063. doi: 10.1093/nar/17.8.3057. [DOI] [PMC free article] [PubMed] [Google Scholar]