Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 217-224 |
| Number of pages | 8 |
| Journal | International Biodeterioration & Biodegradation |
| Volume | 39 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 1997 |
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Serpula lacrymans and the heat-shock response. / Sienkiewicz, N.; Buultjens, T. E. J.; White, Nia A.; Palfreyman, John W.
In: International Biodeterioration & Biodegradation, Vol. 39, No. 2-3, 1997, p. 217-224.Research output: Contribution to journal › Article
TY - JOUR
T1 - Serpula lacrymans and the heat-shock response
AU - Sienkiewicz, N.
AU - Buultjens, T. E. J.
AU - White, Nia A.
AU - Palfreyman, John W.
PY - 1997
Y1 - 1997
N2 - The dry-rot fungus Serpula lacrymans has a maximum growth temperature of 28°C which is an unusual feature in comparison to other Serpula species. This has led to the investigation of S. lacrymans sensitivity to higher temperature regimes with respect to increased thermotolerance and the production of heat-shock proteins (hsps). The strategy employed in this study has been to correlate protein synthesis with thermotolerance and the heat-shock response. Protein profiles generated by one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (1D SDS-PAGE) of fungal colonies exposed to optimal, supraoptimal (sublethal) and lethal temperatures were probed with rabbit anti-GRoEL serum for the presence of the 60-kDa heat-shock protein. The preliminary findings indicate that an important heat-shock protein, a GRoEL analogue, is produced by S. lacrymans and that this basidiomycete undergoes the classic heat-shock response.
AB - The dry-rot fungus Serpula lacrymans has a maximum growth temperature of 28°C which is an unusual feature in comparison to other Serpula species. This has led to the investigation of S. lacrymans sensitivity to higher temperature regimes with respect to increased thermotolerance and the production of heat-shock proteins (hsps). The strategy employed in this study has been to correlate protein synthesis with thermotolerance and the heat-shock response. Protein profiles generated by one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (1D SDS-PAGE) of fungal colonies exposed to optimal, supraoptimal (sublethal) and lethal temperatures were probed with rabbit anti-GRoEL serum for the presence of the 60-kDa heat-shock protein. The preliminary findings indicate that an important heat-shock protein, a GRoEL analogue, is produced by S. lacrymans and that this basidiomycete undergoes the classic heat-shock response.
U2 - 10.1016/S0964-8305(97)00016-4
DO - 10.1016/S0964-8305(97)00016-4
M3 - Article
VL - 39
SP - 217
EP - 224
JO - International Biodeterioration and Biodegradation
JF - International Biodeterioration and Biodegradation
SN - 0964-8305
IS - 2-3
ER -