The Plant Cell, Vol. 14, 1621-1633,
July 2002, Copyright © 2002,
American Society of Plant Biologists
Maize HSP101 Plays Important Roles in Both Induced and Basal Thermotolerance and Primary Root Growth
Jorge Nieto-Sotelo1,a,
Luz María Martíneza,
Georgina Poncea,
Gladys I. Cassaba,
Alejandro Alagónb,
Robert B. Meeleyc,
Jean-Marcel Ribautd and
Runying Yanga
a Department of Plant Molecular Biology, Institute of Biotechnology, National Autonomous University of Mexico, 62250 Cuernavaca, Morelos, Mexico
b Department of Molecular Recognition and Biostructure, Institute of Biotechnology, National Autonomous University of Mexico, 62250 Cuernavaca, Morelos, Mexico
c Trait and Technology Development, Pioneer Hi-Bred International, Inc., Johnston, Iowa 50310
d International Maize and Wheat Improvement Center, Lisboa 27, Apdo Postal 6-641, 06600 Mexico City, Distrito Federal, Mexico
1 To whom correspondence should be addressed. E-mail jorge{at}ibt.unam.mx; fax 52-7-313-9988
HSP101 belongs to the ClpB protein subfamily whose members promote the renaturation of protein aggregates and are essential for the induction of thermotolerance. We found that maize HSP101 accumulated in mature kernels in the absence of heat stress. At optimal temperatures, HSP101 disappeared within the first 3 days after imbibition, although its levels increased in response to heat shock. In embryonic cells, HSP101 concentrated in the nucleus and in some nucleoli. Hsp101 maps near the umc132 and npi280 markers on chromosome 6. Five maize hsp101-m-::Mu1 alleles were isolated. Mutants were null for HSP101 and defective in both induced and basal thermotolerance. Moreover, during the first 3 days after imbibition, primary roots grew faster in the mutants at optimal temperature. Thus, HSP101 is a nucleus-localized protein that, in addition to its role in thermotolerance, negatively influences the growth rate of the primary root. HSP101 is dispensable for proper embryo and whole plant development in the absence of heat stress.
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