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- Title
Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein.
- Authors
Cha, Joon-Yung; Ermawati, Netty; Jung, Min Hee; Su'udi, Mukhamad; Kim, Ki-Yong; Kim, Jae-Yean; Han, Chang-deok; Lee, Kon Ho; Son, Daeyoung
- Abstract
p23 is a heat shock protein 90 (Hsp90) co-chaperone and stabilizes the Hsp90 heterocomplex in mammals and yeast. In this study, we isolated a complementary DNA (cDNA) encoding p23 from orchardgrass ( Dgp23) and characterized its functional roles under conditions of thermal stress. Dgp23 is a 911 bp cDNA with an open reading frame predicted to encode a 180 amino acid protein. Northern analysis showed that expression of Dgp23 transcripts was heat inducible. Dgp23 has a well-conserved p23 domain and interacted with an orchardgrass Hsp90 homolog in vivo, like mammalian and yeast p23 homologs. Recombinant Dgp23 is a small acidic protein with a molecular mass of approximately 27 kDa and p I 4.3. Dgp23 was also shown to function as a chaperone protein by suppression of malate dehydrogenase thermal aggregation. Differential scanning calorimetry thermograms indicated that Dgp23 is a heat-stable protein, capable of increasing the Tm of lysozyme. Moreover, overexpression of Dgp23 in a yeast p23 homolog deletion strain, Δ sba1, increased cell viability. These results suggest that Dgp23 plays a role in thermal stress-tolerance and functions as a co-chaperone of Hsp90 and as a chaperone.
- Subjects
HEAT shock proteins; ANTISENSE DNA; MOLECULAR chaperones; ORCHARD grass; EFFECT of temperature on plants; AMINO acids
- Publication
Cell Stress & Chaperones, 2009, Vol 14, Issue 3, p233
- ISSN
1355-8145
- Publication type
Article
- DOI
10.1007/s12192-008-0077-6