A family of transcripts encoding water channel proteins: tissue-specific expression in the common ice plant.
Seawater-strength salt stress of the ice plant (Mesembryanthemum crystallinum) initially results in wilting, but full turgor is restored within approximately 2 days. We are interested in a mechanistic explanation for this behavior and, as a requisite for in-depth biochemical studies, have begun to analyze gene expression changes in roots coincident with the onset of stress. cDNAs that suggested changes in mRNA amount under stress were found; their deduced amino acid sequences share homologies with proteins of the Mip (major intrinsic protein) gene family and potentially encode aquaporins. One transcript, MipB, was found only in root RNA, whereas two other transcripts, MipA and MipC, were detected in roots and leaves. Transcript levels of MipB were of low abundance. All transcripts declined initially during salt stress but later recovered to at least prestress level. The most drastic decline was in MipA and MipC transcripts. MipA mRNA distribution in roots detected by in situ hybridization indicated that the transcript was present in all cells in the root tip. In the expansion zone of the root where vascular bundles differentiate, MipA transcript amounts were most abundant in the endodermis. In older roots, which had undergone secondary growth, MipA was highly expressed in cell layers surrounding individual xylem strands. MipA was also localized in leaf vascular tissue and, in lower amounts, in mesophyll cells. Transcripts for MipB seemed to be present exclusively in the tip of the root, in a zone before and possibly coincident with the development of a vascular system. MipA- and MipB-encoded proteins expressed in Xenopus oocytes led to increased water permeability. mRNA fluctuations of the most highly expressed MipA and MipC coincided with turgor changes in leaves under stress. As the leaves regained turgor, transcript levels of these water channel proteins increased.
Yamada
S
S
Department of Biochemistry, University of Arizona, Tucson 85721, USA.
Katsuhara
M
M
Kelly
W B
WB
Michalowski
C B
CB
Bohnert
H J
HJ
D000595:Amino Acid Sequence; D000818:Animals; D020346:Aquaporins; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D018076:DNA, Complementary / Q000235:genetics; D015723:Gene Library; D017343:Genes, Plant / Q000235:genetics*; D017403:In Situ Hybridization; D007473:Ion Channels / Q000145:classification / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics; D009865:Oocytes; D010940:Plant Proteins / Q000145:classification / Q000235:genetics*; D010944:Plants / Q000235:genetics*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D014018:Tissue Distribution; D014882:Water-Electrolyte Balance / Q000235:genetics*; D014981:Xenopus
D020346:Aquaporins; D018076:DNA, Complementary; D007473:Ion Channels; D010940:Plant Proteins; D012333:RNA, Messenger; C110065:major intrinsic protein, plant