|
Plant Physiol, July 2000, Vol. 123, pp. 1121-1132
Acquired Thermotolerance and Expression of the
HSP100/ClpB Genes of Lima Bean1
Sharon J.
Keeler,2*
Cynthia M.
Boettger,
Janine G.
Haynes,
Kelly Ann
Kuches,
Marisia M.
Johnson,
Dean L.
Thureen,
Calvin L.
Keeler Jr., and
Sherry L.
Kitto
Department of Plant and Soil Sciences (S.J.K., C.M.B., J.G.H.,
K.A.K., M.M.J., S.L.K.) and Department of Animal and Food Sciences
(C.L.K.), University of Delaware, Newark, Delaware 19717; and E. I. Dupont de Nemours, Delaware Technology Park, Newark, Delaware 19717 (D.L.T.)
Acquired thermotolerance (AT) is the ability of cells to survive a
normally lethal temperature treatment as a consequence of pretreatment
at an elevated but sublethal temperature. In yeast and cyanobacteria,
the expression of the HSP100/ClpB protein is required for the AT
response. To determine whether the HSP100/ClpB protein is associated
with this response in lima bean (Phaseolus lunatus), we have cloned an HSP100/ClpB homolog and
assessed expression of the two gene copies under heat stress
conditions, which induce AT. Transcription of the cytoplasmically
localized HSP100/ClpB protein genes is stringently controlled by heat
stress in both of the laboratory and field heat stress conditions. From
a heat-induced cDNA library, we identified a clone of a putative
chloroplast-targeted (cp) HSP100/ClpB protein gene sequence. The cp
HSP100/ClpB protein genes are constitutively expressed, but transcript
levels increase post-heat stress in laboratory heat stress experiments.
In field conditions the genes for the cp HSP100/ClpB are constitutively expressed. Although we were unable to correlate differences in the
timing of AT response with the expression or genetic structure of the
HSP100/ClpB genes in heat-tolerant or -sensitive varieties of lima
bean, we clearly demonstrate the association of expression of
HSP100/ClpB proteins with heat response in this species.
1
This work was supported in part by the U.S.
Department of Agriculture-National Research Initiative (grant no.
95-37311-2458), by the University of Delaware, College of
Agriculture and Natural Resources Competitive Grants Program, and by
the State of Delaware Advanced Technology Fund.
2
Present address: E. I. Dupont de Nemours, Building
300/304, Glasgow, Newark, DE 19702.
*
Corresponding author; e-mail sharon.j.keeler{at}usa.dupont.com;
fax 302-366-6602.
© 2000 American Society of Plant Physiologists
This article has been cited by other articles:

|
 |

|
 |
 
D. Barua and S. A. Heckathorn
The interactive effects of light and temperature on heat-shock protein accumulation in Solidago altissima (Asteraceae) in the field and laboratory
Am. J. Botany,
January 1, 2006;
93(1):
102 - 109.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. Otani, T. Ueki, S. Kozuka, M. Segawa, K. Sano, and S. Inouye
Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus
J. Bacteriol.,
August 1, 2005;
187(15):
5236 - 5241.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. L.E. Sjogren, T. M. MacDonald, S. Sutinen, and A. K. Clarke
Inactivation of the clpC1 Gene Encoding a Chloroplast Hsp100 Molecular Chaperone Causes Growth Retardation, Leaf Chlorosis, Lower Photosynthetic Activity, and a Specific Reduction in Photosystem Content
Plant Physiology,
December 1, 2004;
136(4):
4114 - 4126.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. Nieto-Sotelo, L. M. Martinez, G. Ponce, G. I. Cassab, A. Alagon, R. B. Meeley, J.-M. Ribaut, and R. Yang
Maize HSP101 Plays Important Roles in Both Induced and Basal Thermotolerance and Primary Root Growth
PLANT CELL,
July 1, 2002;
14(7):
1621 - 1633.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M.-J. Eriksson, J. Schelin, E. Miskiewicz, and A. K. Clarke
Novel Form of ClpB/HSP100 Protein in the Cyanobacterium Synechococcus
J. Bacteriol.,
December 15, 2001;
183(24):
7392 - 7396.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|