Advanced

Trimming Down a Protein Structure to Its Bare Foldons SPATIAL ORGANIZATION OF THE COOPERATIVE UNIT

Haglund, Ellinor; Danielsson, Jens; Kadhirvel, Saraboji LU ; Lindberg, Magnus O.; Logan, Derek LU and Oliveberg, Mikael (2012) In Journal of Biological Chemistry 287(4). p.2731-2738
Abstract
Folding of the ribosomal protein S6 is a malleable process controlled by two competing, and partly overlapping, folding nuclei. Together, these nuclei extend over most of the S6 structure, except the edge strand beta 2, which is consistently missing in the folding transition states; despite being part of the S6 four-stranded sheet, beta 2 seems not to be part of the cooperative unit of the protein. The question is then whether beta 2 can be removed from the S6 structure without compromising folding cooperativity or native state integrity. To investigate this, we constructed a truncated variant of S6 lacking beta 2, reducing the size of the protein from 96 to 76 residues (S6(Delta beta 2)). The new S6 variant expresses well in Escherichia... (More)
Folding of the ribosomal protein S6 is a malleable process controlled by two competing, and partly overlapping, folding nuclei. Together, these nuclei extend over most of the S6 structure, except the edge strand beta 2, which is consistently missing in the folding transition states; despite being part of the S6 four-stranded sheet, beta 2 seems not to be part of the cooperative unit of the protein. The question is then whether beta 2 can be removed from the S6 structure without compromising folding cooperativity or native state integrity. To investigate this, we constructed a truncated variant of S6 lacking beta 2, reducing the size of the protein from 96 to 76 residues (S6(Delta beta 2)). The new S6 variant expresses well in Escherichia coli and has a well dispersed heteronuclear single quantum correlation spectrum and a perfectly wild-type-like crystal structure, but with a smaller three-stranded beta-sheet. Moreover, S6(Delta beta 2) displays an archetypical v-shaped chevron plot with decreased slope of the unfolding limb, as expected from a protein with maintained folding cooperativity and reduced size. The results support the notion that foldons, as defined by the structural distribution of the folding nuclei, represent a property-based level of hierarchy in the build-up of larger protein structures and suggest that the role of beta 2 in S6 is mainly in intermolecular binding, consistent with the position of this strand in the ribosomal assembly. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
287
issue
4
pages
2731 - 2738
publisher
ASBMB
external identifiers
  • wos:000300292300044
  • scopus:84856068609
ISSN
1083-351X
DOI
10.1074/jbc.M111.312447
language
English
LU publication?
yes
id
ccaa6ab4-581c-46b2-b2d5-0a3482d1a399 (old id 2403220)
date added to LUP
2012-03-27 14:41:14
date last changed
2017-01-01 03:04:37
@article{ccaa6ab4-581c-46b2-b2d5-0a3482d1a399,
  abstract     = {Folding of the ribosomal protein S6 is a malleable process controlled by two competing, and partly overlapping, folding nuclei. Together, these nuclei extend over most of the S6 structure, except the edge strand beta 2, which is consistently missing in the folding transition states; despite being part of the S6 four-stranded sheet, beta 2 seems not to be part of the cooperative unit of the protein. The question is then whether beta 2 can be removed from the S6 structure without compromising folding cooperativity or native state integrity. To investigate this, we constructed a truncated variant of S6 lacking beta 2, reducing the size of the protein from 96 to 76 residues (S6(Delta beta 2)). The new S6 variant expresses well in Escherichia coli and has a well dispersed heteronuclear single quantum correlation spectrum and a perfectly wild-type-like crystal structure, but with a smaller three-stranded beta-sheet. Moreover, S6(Delta beta 2) displays an archetypical v-shaped chevron plot with decreased slope of the unfolding limb, as expected from a protein with maintained folding cooperativity and reduced size. The results support the notion that foldons, as defined by the structural distribution of the folding nuclei, represent a property-based level of hierarchy in the build-up of larger protein structures and suggest that the role of beta 2 in S6 is mainly in intermolecular binding, consistent with the position of this strand in the ribosomal assembly.},
  author       = {Haglund, Ellinor and Danielsson, Jens and Kadhirvel, Saraboji and Lindberg, Magnus O. and Logan, Derek and Oliveberg, Mikael},
  issn         = {1083-351X},
  language     = {eng},
  number       = {4},
  pages        = {2731--2738},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Trimming Down a Protein Structure to Its Bare Foldons SPATIAL ORGANIZATION OF THE COOPERATIVE UNIT},
  url          = {http://dx.doi.org/10.1074/jbc.M111.312447},
  volume       = {287},
  year         = {2012},
}