S. Yamada et al., A FAMILY OF TRANSCRIPTS ENCODING WATER CHANNEL PROTEINS - TISSUE-SPECIFIC EXPRESSION IN THE COMMON ICE PLANT, The Plant cell, 7(8), 1995, pp. 1129-1142
Seawater-strength salt stress of the ice plant (Mesembryanthemum cryst
allinum) initially results in wilting, but full turgor is restored wit
hin similar to 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 wi
th the onset of stress. cDNAs that suggested changes in mRNA amount un
der stress were found; their deduced amino acid sequences share homolo
gies with proteins of the Mip (major intrinsic protein) gene family an
d potentially encode aquaporins. One transcript, MipB, was found only
in root RNA, whereas two other transcripts, MipA and MipC, were detect
ed in roots and leaves. Transcript levels of MipB were of low abundanc
e. All transcripts declined initially during salt stress but later rec
overed to at least prestress level. The most drastic decline was in Mi
pA and MipC transcripts. MipA mRNA distribution in roots detected by i
n situ hybridization indicated that the transcript was present in all
cells in the root tip. In the expansion zone of the root where vascula
r 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 lowe
r amounts, in mesophyll cells. Transcripts for MipB seemed to be prese
nt exclusively in the tip of the root, in a zone before and possibly c
oincident with the development of a vascular system. MipA- and MipB-en
coded proteins expressed in Xenopus oocytes led to increased water per
meability. mRNA fluctuations of the most highly expressed MipA and Mip
C coincided with turgor changes in leaves under stress. As the leaves
regained turgor, transcript levels of these water channel proteins inc
reased.