Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo.
Small heat-stress proteins (sHsps) are the most abundant stress-induced proteins with up to 20 different members in higher plants. In the cytoplasm, two different classes can be distinguished. Two cDNA clones from tomato Lycopersicon peruvianum (L.) Mill., each coding for one of the cytoplasmic sHsp subfamilies, were analyzed with respect to their transcript and protein expression, genome organization and chaperone activity. Neither type was present under control conditions but both appeared upon heat stress and in mature fruits. Expression of the class II transcript was found to be induced at slightly lower temperatures than the class I transcript. Protein analysis using class-specific antibodies revealed an identical expression pattern of both corresponding proteins. Transient expression in an Arabidopsis thaliana (L.) Heynh. cell culture showed that, despite the difference in their amino acid sequence, both classes are functionally active as chaperones in vivo, as shown by their ability to prevent thermal inactivation of firefly luciferase in a cellular environment.
Löw
D
D
Molekulare Zellbiologie, Biozentrum, Goethe Universität, Frankfurt am Main, Germany.
Brändle
K
K
Nover
L
L
Forreiter
C
C
D000595:Amino Acid Sequence; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology*; D018551:Solanum lycopersicum / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010940:Plant Proteins