Small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase
Åhrman, Emma LU ; Gustavsson, Niklas LU ; Hultschig, Claus ; Boelens, Wilbert C. and Emanuelsson, Cecilia LU
(2007)
In Extremophiles
11(5).
p.659-666
- Abstract
- Citrate synthase (CS) is often used in chaperone assays since this thermosensitive enzyme aggregates at moderately increased temperatures. Small heat shock proteins (sHsps) are molecular chaperones specialized in preventing the aggregation of other proteins, termed substrate proteins, under conditions of transient heat stress. To investigate the mechanism whereby sHsps bind to and stabilize a substrate protein, we here used peptide array screening covering the sequence of porcine CS (P00889). Strong binding of sHsps was detected to a peptide corresponding to the most N-terminal alpha-helix in CS (amino acids Leu(13) to Gln(27)). The N-terminal alpha-helices in the CS dimer intertwine with the C-terminus in the other subunit and together... (More)
- Citrate synthase (CS) is often used in chaperone assays since this thermosensitive enzyme aggregates at moderately increased temperatures. Small heat shock proteins (sHsps) are molecular chaperones specialized in preventing the aggregation of other proteins, termed substrate proteins, under conditions of transient heat stress. To investigate the mechanism whereby sHsps bind to and stabilize a substrate protein, we here used peptide array screening covering the sequence of porcine CS (P00889). Strong binding of sHsps was detected to a peptide corresponding to the most N-terminal alpha-helix in CS (amino acids Leu(13) to Gln(27)). The N-terminal alpha-helices in the CS dimer intertwine with the C-terminus in the other subunit and together form a stem-like structure which is protruding from the CS dimer. This stem-like structure is absent in thermostable forms of CS from thermophilic archaebacteria like Pyrococcus furiosus and Sulfolobus solfatacarium. These data therefore suggest that thermostabilization of thermosensitive CS by sHsps is achieved by stabilization of the C- and N-terminae in the protruding thermosensitive softspot, which is absent in thermostable forms of the CS dimer. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/688052
- author
- Åhrman, Emma
LU
; Gustavsson, Niklas
LU
; Hultschig, Claus
; Boelens, Wilbert C.
and Emanuelsson, Cecilia
LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- stability, protein, protein-protein interactions, heat stress, chaperones, thermosensitivity
- in
- Extremophiles
- volume
- 11
- issue
- 5
- pages
- 659 - 666
- publisher
- Springer
- external identifiers
-
- wos:000249119300002
- scopus:34548309201
- ISSN
- 1433-4909
- DOI
- 10.1007/s00792-007-0080-3
- language
- English
- LU publication?
- yes
- id
- 13f62cb1-3b92-4a47-82ac-3046f49810c9 (old id 688052)
- date added to LUP
- 2016-04-01 11:38:03
- date last changed
- 2022-01-26 07:54:21
@article{13f62cb1-3b92-4a47-82ac-3046f49810c9,
abstract = {{Citrate synthase (CS) is often used in chaperone assays since this thermosensitive enzyme aggregates at moderately increased temperatures. Small heat shock proteins (sHsps) are molecular chaperones specialized in preventing the aggregation of other proteins, termed substrate proteins, under conditions of transient heat stress. To investigate the mechanism whereby sHsps bind to and stabilize a substrate protein, we here used peptide array screening covering the sequence of porcine CS (P00889). Strong binding of sHsps was detected to a peptide corresponding to the most N-terminal alpha-helix in CS (amino acids Leu(13) to Gln(27)). The N-terminal alpha-helices in the CS dimer intertwine with the C-terminus in the other subunit and together form a stem-like structure which is protruding from the CS dimer. This stem-like structure is absent in thermostable forms of CS from thermophilic archaebacteria like Pyrococcus furiosus and Sulfolobus solfatacarium. These data therefore suggest that thermostabilization of thermosensitive CS by sHsps is achieved by stabilization of the C- and N-terminae in the protruding thermosensitive softspot, which is absent in thermostable forms of the CS dimer.}},
author = {{Åhrman, Emma and Gustavsson, Niklas and Hultschig, Claus and Boelens, Wilbert C. and Emanuelsson, Cecilia}},
issn = {{1433-4909}},
keywords = {{stability; protein; protein-protein interactions; heat stress; chaperones; thermosensitivity}},
language = {{eng}},
number = {{5}},
pages = {{659--666}},
publisher = {{Springer}},
series = {{Extremophiles}},
title = {{Small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase}},
url = {{http://dx.doi.org/10.1007/s00792-007-0080-3}},
doi = {{10.1007/s00792-007-0080-3}},
volume = {{11}},
year = {{2007}},
}