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Plant Physiol, November 2001, Vol. 127, pp. 777-791
Developmental and Thermal Regulation of the Maize Heat Shock
Protein, HSP1011
Todd E.
Young,2
Jun
Ling,2
C. Jane
Geisler-Lee,2
Robert L.
Tanguay,3
Christian
Caldwell, and
Daniel R.
Gallie*
Department of Biochemistry, University of California, Riverside,
California 92521-0129
The plant heat stress protein, Hsp101, and the yeast
ortholog, Hsp104, are required to confer thermotolerance in plants and yeast (Saccharomyces cerevisiae), respectively. In addition
to its function during stress, Hsp101 is developmentally regulated in
plants although its function during development is not known. To
determine how the expression of Hsp101 is regulated in cereals, we
investigated the Hsp101 expression profile in developing maize (Zea mays). Hsp101 protein was most abundant in the
developing tassel, ear, silks, endosperm, and embryo. It was less
abundant in the vegetative and floral meristematic regions and was
present at only a low level in the anthers and tassel at anthesis,
mature pollen, roots, and leaves. As expected, heat treatment resulted in an increase in the level of Hsp101 protein in several organs. In
expanding foliar leaves, husk leaves, the tassel at the premeiosis stage of development, or pre-anthesis anthers, however, the
heat-mediated increase in protein was not accompanied by an equivalent
increase in mRNA. In contrast, the level of Hsp101 transcript increased in the tassel at anthesis following a heat stress without an increase in Hsp101 protein. In other organs such as the vegetative and floral
meristematic regions, fully expanded foliar leaves, the young ear, and
roots, the heat-induced increase in Hsp101 protein was accompanied by a
corresponding increase in Hsp101 transcript level. However, anthers at
anthesis, mature pollen, developing endosperm, and embryos largely
failed to mount a heat stress response at the level of Hsp101 protein
or mRNA, indicating that Hsp101 expression is not heat inducible in
these organs. In situ RNA localization analysis revealed that Hsp101
mRNA accumulated in the subaleurone and aleurone of developing kernels
and was highest in the root cap meristem and quiescent center of
heat-stressed roots. These data suggest an organ-specific control of
Hsp101 expression during development and following a heat stress
through mechanisms that may include posttranscriptional
regulation.
1
This work was supported by the U.S. Department
of Agriculture (grant no. NRICGP 00-35301-9086) and by the National
Science Foundation (grant no. MCB-9816657).
2
These authors contributed equally to the paper.
3
Present address: Department of Pharmaceutical
Sciences, University of Colorado Health Sciences Center, Madison, WI 53706.
*
Corresponding author; e-mail drgallie{at}citrus.ucr.edu; fax
909-787-3590.
© 2001 American Society of Plant Physiologists
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