Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1996 Nov;112(3):1391–1396. doi: 10.1104/pp.112.3.1391

cDNA isolation and gene expression of the maize annexins p33 and p35.

N H Battey 1, N C James 1, A J Greenland 1
PMCID: PMC158068  PMID: 8938425

Abstract

The isolation, cloning, and sequencing of two full-length cDNAs corresponding to the root tip forms of the maize (Zea mays L. cv Clipper) annexins p33 and p35 are described. These are the first complete sequences for the widely reported doublet of plant annexins. The predicted sequences can be divided into four repeat domains characteristic of the annexin family, but Ca2+ binding by the type-II site typical of annexins would be predicted to occur only in repeats 1 and 4. This reduced number of sites is consistent with previously reported biochemical data indicating a high Ca2+ requirement for membrane association. Although the two annexins are very similar (80% amino acid identity), their genes are quite distinct, as demonstrated by their different 3' noncoding regions and Southern blotting. The predicted sequences of the root tip proteins are very similar to regions known from peptide sequencing of the coleoptile proteins. Because a rather small gene family is indicated, the implication is that there may be less functional diversity than in animal cells. Furthermore, the sequence data clearly show that plant annexins form a very distinct group compared with those from other kingdoms.

Full Text

The Full Text of this article is available as a PDF (1.7 MB).

Selected References

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

  1. Blackbourn H. D., Barker P. J., Huskisson N. S., Battey N. H. Properties and partial protein sequence of plant annexins. Plant Physiol. 1992 Jul;99(3):864–871. doi: 10.1104/pp.99.3.864. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Calvert C. M., Gant S. J., Bowles D. J. Tomato annexins p34 and p35 bind to F-actin and display nucleotide phosphodiesterase activity inhibited by phospholipid binding. Plant Cell. 1996 Feb;8(2):333–342. doi: 10.1105/tpc.8.2.333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fiedler K., Lafont F., Parton R. G., Simons K. Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J Cell Biol. 1995 Mar;128(6):1043–1053. doi: 10.1083/jcb.128.6.1043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Huber R., Schneider M., Mayr I., Römisch J., Paques E. P. The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. FEBS Lett. 1990 Nov 26;275(1-2):15–21. doi: 10.1016/0014-5793(90)81428-q. [DOI] [PubMed] [Google Scholar]
  5. Ikonen E., Tagaya M., Ullrich O., Montecucco C., Simons K. Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell. 1995 May 19;81(4):571–580. doi: 10.1016/0092-8674(95)90078-0. [DOI] [PubMed] [Google Scholar]
  6. Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984 Jan 25;12(2):857–872. doi: 10.1093/nar/12.2.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Larkin J. C., Hunsperger J. P., Culley D., Rubenstein I., Silflow C. D. The organization and expression of a maize ribosomal protein gene family. Genes Dev. 1989 Apr;3(4):500–509. doi: 10.1101/gad.3.4.500. [DOI] [PubMed] [Google Scholar]
  8. Luecke H., Chang B. T., Mailliard W. S., Schlaepfer D. D., Haigler H. T. Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature. 1995 Nov 30;378(6556):512–515. doi: 10.1038/378512a0. [DOI] [PubMed] [Google Scholar]
  9. McClung A. D., Carroll A. D., Battey N. H. Identification and characterization of ATPase activity associated with maize (Zea mays) annexins. Biochem J. 1994 Nov 1;303(Pt 3):709–712. doi: 10.1042/bj3030709. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Proust J., Houlné G., Schantz M. L., Schantz R. Characterization and gene expression of an annexin during fruit development in Capsicum annuum. FEBS Lett. 1996 Apr 1;383(3):208–212. doi: 10.1016/0014-5793(96)00252-9. [DOI] [PubMed] [Google Scholar]
  11. Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1(8):945–951. doi: 10.1002/j.1460-2075.1982.tb01276.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Weng X., Luecke H., Song I. S., Kang D. S., Kim S. H., Huber R. Crystal structure of human annexin I at 2.5 A resolution. Protein Sci. 1993 Mar;2(3):448–458. doi: 10.1002/pro.5560020317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wice B. M., Gordon J. I. A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. J Cell Biol. 1992 Jan;116(2):405–422. doi: 10.1083/jcb.116.2.405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wilkinson J. Q., Lanahan M. B., Conner T. W., Klee H. J. Identification of mRNAs with enhanced expression in ripening strawberry fruit using polymerase chain reaction differential display. Plant Mol Biol. 1995 Mar;27(6):1097–1108. doi: 10.1007/BF00020883. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES