The discovery of chaperonins | Nature Structural & Molecular Biology

The discovery of chaperonins | Nature Structural & Molecular Biology

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Access through your institution Buy or subscribe Both the editorial in this issue of _Nature Structural Biology_ and the paper on page 1132 focus on protein folding research. Here we note that our understanding of the general properties of folding reactions _in vivo_ took a major step forward in the late 1980s, when research from several disparate fields revealed the widespread function of the GroEL (hsp60) related proteins, members of the class of chaperones known as the chaperonins. GroEL is required for the correct assembly of the oligomeric structure that connects the head to the tail of λ phage. It was identified in 1972–1973 by genetic approaches, in the search for factors involved in the replication of bacteriophages1,2 and its name reflects this history: 'Gro' stands for phage growth; 'E' indicates that the growth defect can be overcome by a mutation in the phage head gene E; and 'L' stands for 'large subunit'. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive 12 print issues and online access $209.00 per year only $17.42 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support REFERENCES * Georgopoulos, C., Hendrix, R.W., Casjens, S.R. & Kaiser, A.D. _ J. Mol. Biol._ 76, 45–60 (1973). Article  CAS  Google Scholar  * Sternberg, N. _ J. Mol. Biol._ 76, 25–44 (1973). Article  CAS  Google Scholar  * Ellis, R.J. _ Science_ 250, 954–959 ( 1990). Article  CAS  Google Scholar  * Hemmingsen, S.M. _ et al._ _Nature_ 333, 330–334 (1988). Article  CAS  Google Scholar  * Cheng, M.Y. _ et al._ _Nature_ 337, 620–625 (1989). Article  CAS  Google Scholar  * Reading, D.S., Hallberg, R.L. & Myers, A.M. _Nature_ 337, 655– 659 (1989). Article  CAS  Google Scholar  * Willison, K.R. & Horwich, A.L In _The chaperonins._ (ed. Ellis, R.J.) 107–136 (Academic Press, Inc., San Diego, California; 1996). Book  Google Scholar  * Osterman, J., Horwich, A.L., Neupert, W. & Hartl, F.-U. _ Nature_ 341, 125–130 ( 1989). Article  Google Scholar  Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Tracy Smith Authors * Tracy Smith View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Smith, T. The discovery of chaperonins. _Nat Struct Mol Biol_ 6, 1090 (1999). https://doi.org/10.1038/70015 Download citation * Issue Date: December 1999 * DOI: https://doi.org/10.1038/70015 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to clipboard Provided by the Springer Nature SharedIt content-sharing initiative

Access through your institution Buy or subscribe Both the editorial in this issue of _Nature Structural Biology_ and the paper on page 1132 focus on protein folding research. Here we note


that our understanding of the general properties of folding reactions _in vivo_ took a major step forward in the late 1980s, when research from several disparate fields revealed the


widespread function of the GroEL (hsp60) related proteins, members of the class of chaperones known as the chaperonins. GroEL is required for the correct assembly of the oligomeric structure


that connects the head to the tail of λ phage. It was identified in 1972–1973 by genetic approaches, in the search for factors involved in the replication of bacteriophages1,2 and its name


reflects this history: 'Gro' stands for phage growth; 'E' indicates that the growth defect can be overcome by a mutation in the phage head gene E; and 'L'


stands for 'large subunit'. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive


12 print issues and online access $209.00 per year only $17.42 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be


subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support


REFERENCES * Georgopoulos, C., Hendrix, R.W., Casjens, S.R. & Kaiser, A.D. _ J. Mol. Biol._ 76, 45–60 (1973). Article  CAS  Google Scholar  * Sternberg, N. _ J. Mol. Biol._ 76, 25–44


(1973). Article  CAS  Google Scholar  * Ellis, R.J. _ Science_ 250, 954–959 ( 1990). Article  CAS  Google Scholar  * Hemmingsen, S.M. _ et al._ _Nature_ 333, 330–334 (1988). Article  CAS 


Google Scholar  * Cheng, M.Y. _ et al._ _Nature_ 337, 620–625 (1989). Article  CAS  Google Scholar  * Reading, D.S., Hallberg, R.L. & Myers, A.M. _Nature_ 337, 655– 659 (1989). Article 


CAS  Google Scholar  * Willison, K.R. & Horwich, A.L In _The chaperonins._ (ed. Ellis, R.J.) 107–136 (Academic Press, Inc., San Diego, California; 1996). Book  Google Scholar  *


Osterman, J., Horwich, A.L., Neupert, W. & Hartl, F.-U. _ Nature_ 341, 125–130 ( 1989). Article  Google Scholar  Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Tracy


Smith Authors * Tracy Smith View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS


ARTICLE Smith, T. The discovery of chaperonins. _Nat Struct Mol Biol_ 6, 1090 (1999). https://doi.org/10.1038/70015 Download citation * Issue Date: December 1999 * DOI:


https://doi.org/10.1038/70015 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently


available for this article. Copy to clipboard Provided by the Springer Nature SharedIt content-sharing initiative