Characterization of orchardgrass p23, a flowering plant Hsp90 cohort proteinopen access
- 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
- Issue Date
- May-2009
- Publisher
- SPRINGER
- Keywords
- Chaperone; Co-chaperone; Hsp90; p23; Orchardgrass; Heat stress; Thermotolerance
- Citation
- CELL STRESS & CHAPERONES, v.14, no.3, pp.233 - 243
- Indexed
- SCIE
SCOPUS
- Journal Title
- CELL STRESS & CHAPERONES
- Volume
- 14
- Number
- 3
- Start Page
- 233
- End Page
- 243
- URI
- https://scholarworks.bwise.kr/gnu/handle/sw.gnu/26311
- DOI
- 10.1007/s12192-008-0077-6
- ISSN
- 1355-8145
- 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 pI 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 T (m) of lysozyme. Moreover, overexpression of Dgp23 in a yeast p23 homolog deletion strain, Delta 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.
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Collections - 농업생명과학대학 > 식물의학과 > Journal Articles
- College of Medicine > Department of Medicine > Journal Articles
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