cDNA isolation and gene expression of the maize annexins p33 and p35.
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.
Battey
N H
NH
Zeneca Agrochemicals, Jealott's Hill Research Station, Bracknell, United Kingdom. n.h.battey@rdg.ac.uk
James
N C
NC
Greenland
A J
AJ
D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins / Q000096:biosynthesis* / Q000737:chemistry; D018076:DNA, Complementary / Q000302:isolation & purification*; D017343:Genes, Plant; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D010940:Plant Proteins / Q000096:biosynthesis / Q000737:chemistry; D018517:Plant Roots; D017386:Sequence Homology, Amino Acid; D003313:Zea mays / Q000235:genetics / Q000378:metabolism*
D017302:Annexins; D018076:DNA, Complementary; D010940:Plant Proteins