In ‘Molecular mechanisms of canalization: Hsp90 and beyond’ the authors explain that Hsp90 acts as a chaperone, ensuring proper folding of client proteins involved in cellular function and phenotype. In the absence of Hsp90 the client proteins become unstable and are rapidly degraded. Hsp90 provides protection against environmental stresses and allows the production of a stable phenotype (canalisation). This important function is why Hsp90 has been discovered in all eukaryotes studied so far.
So are the proteins it protects actually important?
Studies have shown that in plants Hsp90 has a close association with R-proteins which produce localised cell death when activated by pathogen-specific effecter molecules. This as well as involvement in light perception, seedling etiolation, and gravitropism make Hsp90 an important chaperone in plants.
So Hsp90 is certainly important in the heat shock response of organisms, but it appears that it has a range of important functions, in a wide variety of organisms.
Queitsch, C. S. (2002). Nature , 618-624.
QUEITSCH, N. S. (2007). Molecular mechanisms of canalization: Hsp90 and beyond. Journl of Bioscience , 457-463.
Rutherford, S. L. (1998). Nature , 336-342.
So Hsp90 is certainly important in the heat shock response of organisms, but it appears that it has a range of important functions, in a wide variety of organisms.
Queitsch, C. S. (2002). Nature , 618-624.
QUEITSCH, N. S. (2007). Molecular mechanisms of canalization: Hsp90 and beyond. Journl of Bioscience , 457-463.
Rutherford, S. L. (1998). Nature , 336-342.
