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Hsp90 as a capacitor for morphological evolution
Author(s): Rutherford SL, Lindquist S
Source: NATURE    Volume: 396    Issue: 6709    Pages: 336-342    Published: NOV 26 1998  
Times Cited: 723     References: 37     
Abstract: The heat-shock protein Hsp90 supports diverse but specific signal transducers and lies at the interface of several developmental pathways. We report here that when Drosophila Hsp90 is mutant or pharmacologically Impaired, phenotypic variation affecting nearly any adult structure is produced, with specific variants depending on the genetic background and occurring both in laboratory strains and in wild populations. Multiple, previously silent, genetic determinants produced these variants and, when enriched by selection, they rapidly became independent of the Hsp90 mutation, Therefore, widespread variation affecting morphogenic pathways exists in nature, but is usually silent; Hsp90 buffers this variation, allowing it to accumulate under neutral conditions, When Hsp90 buffering is compromised, for example by temperature, cryptic variants are expressed and selection can lead to the continued expression of these traits, even when Hsp90 function is restored. This provides a plausible mechanism for promoting evolutionary change in otherwise entrenched developmental processes.
Document Type: Article
Language: English
Reprint Address: Lindquist, S (reprint author), Univ Calif Irvine, Ctr Dev Biol, 4205 Biol Sci 2, Irvine, CA 92697 USA
Addresses:
1. Univ Chicago, Howard Hughes Med Inst, Chicago, IL 60637 USA
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: 142MJ
ISSN: 0028-0836
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