Details
| Original language | English |
|---|---|
| Pages (from-to) | 90-98 |
| Number of pages | 9 |
| Journal | Journal of structural biology |
| Volume | 146 |
| Issue number | 1-2 |
| Publication status | Published - Apr 2004 |
| Externally published | Yes |
Abstract
AAA+ proteins remodel target substrates in an ATP-dependent manner, an activity that is of central importance for a plethora of cellular processes. While sharing a similar hexameric structure AAA+ proteins must exhibit differences in substrate recognition to fulfil their diverse biological functions. Here we describe strategies of AAA+ proteins to ensure substrate specificity. AAA domains can directly mediate substrate recognition, however, in general extra domains, added to the core AAA domain, control substrate interaction. Such extra domains may either directly recognize substrates or serve as a platform for adaptor proteins, which transfer bound substrates to their AAA+ partner proteins. The positioning of adaptor proteins in substrate recognition can enable them to control the activity of their partner proteins by coupling AAA+ protein activation to substrate availability.
Keywords
- AAA+ superfamily, Adaptor protein, Chaperone, Protease, Substrate specificity
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Journal of structural biology, Vol. 146, No. 1-2, 04.2004, p. 90-98.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Broad yet high substrate specificity
T2 - The challenge of AAA+ proteins
AU - Mogk, Axel
AU - Dougan, David
AU - Weibezahn, Jimena
AU - Schlieker, Christian
AU - Turgay, Kursad
AU - Bukau, Bernd
N1 - Funding information: This work was supported by Grants from the DFG (Leibnizprogramm Bu617/14-1 and Bu617/15-1) and the Fond der Chemischen Industrie to B.B. and A.M.
PY - 2004/4
Y1 - 2004/4
N2 - AAA+ proteins remodel target substrates in an ATP-dependent manner, an activity that is of central importance for a plethora of cellular processes. While sharing a similar hexameric structure AAA+ proteins must exhibit differences in substrate recognition to fulfil their diverse biological functions. Here we describe strategies of AAA+ proteins to ensure substrate specificity. AAA domains can directly mediate substrate recognition, however, in general extra domains, added to the core AAA domain, control substrate interaction. Such extra domains may either directly recognize substrates or serve as a platform for adaptor proteins, which transfer bound substrates to their AAA+ partner proteins. The positioning of adaptor proteins in substrate recognition can enable them to control the activity of their partner proteins by coupling AAA+ protein activation to substrate availability.
AB - AAA+ proteins remodel target substrates in an ATP-dependent manner, an activity that is of central importance for a plethora of cellular processes. While sharing a similar hexameric structure AAA+ proteins must exhibit differences in substrate recognition to fulfil their diverse biological functions. Here we describe strategies of AAA+ proteins to ensure substrate specificity. AAA domains can directly mediate substrate recognition, however, in general extra domains, added to the core AAA domain, control substrate interaction. Such extra domains may either directly recognize substrates or serve as a platform for adaptor proteins, which transfer bound substrates to their AAA+ partner proteins. The positioning of adaptor proteins in substrate recognition can enable them to control the activity of their partner proteins by coupling AAA+ protein activation to substrate availability.
KW - AAA+ superfamily
KW - Adaptor protein
KW - Chaperone
KW - Protease
KW - Substrate specificity
UR - http://www.scopus.com/inward/record.url?scp=1642363290&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2003.10.009
DO - 10.1016/j.jsb.2003.10.009
M3 - Article
C2 - 15037240
AN - SCOPUS:1642363290
VL - 146
SP - 90
EP - 98
JO - Journal of structural biology
JF - Journal of structural biology
SN - 1047-8477
IS - 1-2
ER -