Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 947-957 |
| Seitenumfang | 11 |
| Fachzeitschrift | Plant molecular biology |
| Jahrgang | 56 |
| Ausgabenummer | 6 |
| Publikationsstatus | Veröffentlicht - 7 Apr. 2005 |
Abstract
We report the identification by two hybrid screens of two novel similar proteins, called Arabidopsis thaliana gamma carbonic anhydrase like1 and 2 (AtγCAL1 and AtγCAL2), that interact specifically with putative Arabidopsis thaliana gamma Carbonic Anhydrase (AtγCA) proteins in plant mitochondria. The interaction region that was located in the N-terminal 150 amino acids of mature AtγCA and AtγCA like proteins represents a new interaction domain. In vitro experiments indicate that these proteins are imported into mitochondria and are associated with mitochondrial complex I as AtγCAs. All plant species analyzed contain both AtγCA and AtγCAL sequences indicating that these genes were conserved throughout plant evolution. Structural modeling of AtγCAL sequences show a deviation of functionally important active site residues with respect to γCAs but could form active interfaces in the interaction with AtγCAs. We postulate a CA complex tightly associated to plant mitochondrial complex.
ASJC Scopus Sachgebiete
- Agrar- und Biowissenschaften (insg.)
- Agronomie und Nutzpflanzenwissenschaften
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
- Agrar- und Biowissenschaften (insg.)
- Pflanzenkunde
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in: Plant molecular biology, Jahrgang 56, Nr. 6, 07.04.2005, S. 947-957.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Gamma carbonic anhydrase like complex interact with plant mitochondrial complex I
AU - Perales, Mariano
AU - Parisi, Gustavo
AU - Fornasari, María Silvina
AU - Colaneri, Alejandro
AU - Villarreal, Fernando
AU - González-Schain, Nahuel
AU - Echave, Julián
AU - Gómez-Casati, Diego
AU - Braun, Hans Peter
AU - Araya, Alejandro
AU - Zabaleta, Eduardo
N1 - Funding information: We would like to thank Dr. Jörg Kudla for helps in performing two hybrid screens and Mr. José Luis Burgos (CIC, Argentina) for excellent technical assistance. This work was supported in part by ANPCyT (05008, 09538 and 0111265) (Argentina), Fundación Antorchas-DAAD (Germany-Argentina), ECOS-Sud, (A00B01) (France-Argentina), Universidad Nacional de Quilmes, Third World Academy of Sciences, Fundacion Antorchas and the DFG (grant BR 1829-7/1). EJ, ZE and GCD are members of the National Research Council (CONICET). PM (ANPCyT, Argentina) and CA (CONICET, Argentina) are doctoral fellows and this work is part of their doctoral theses.
PY - 2005/4/7
Y1 - 2005/4/7
N2 - We report the identification by two hybrid screens of two novel similar proteins, called Arabidopsis thaliana gamma carbonic anhydrase like1 and 2 (AtγCAL1 and AtγCAL2), that interact specifically with putative Arabidopsis thaliana gamma Carbonic Anhydrase (AtγCA) proteins in plant mitochondria. The interaction region that was located in the N-terminal 150 amino acids of mature AtγCA and AtγCA like proteins represents a new interaction domain. In vitro experiments indicate that these proteins are imported into mitochondria and are associated with mitochondrial complex I as AtγCAs. All plant species analyzed contain both AtγCA and AtγCAL sequences indicating that these genes were conserved throughout plant evolution. Structural modeling of AtγCAL sequences show a deviation of functionally important active site residues with respect to γCAs but could form active interfaces in the interaction with AtγCAs. We postulate a CA complex tightly associated to plant mitochondrial complex.
AB - We report the identification by two hybrid screens of two novel similar proteins, called Arabidopsis thaliana gamma carbonic anhydrase like1 and 2 (AtγCAL1 and AtγCAL2), that interact specifically with putative Arabidopsis thaliana gamma Carbonic Anhydrase (AtγCA) proteins in plant mitochondria. The interaction region that was located in the N-terminal 150 amino acids of mature AtγCA and AtγCA like proteins represents a new interaction domain. In vitro experiments indicate that these proteins are imported into mitochondria and are associated with mitochondrial complex I as AtγCAs. All plant species analyzed contain both AtγCA and AtγCAL sequences indicating that these genes were conserved throughout plant evolution. Structural modeling of AtγCAL sequences show a deviation of functionally important active site residues with respect to γCAs but could form active interfaces in the interaction with AtγCAs. We postulate a CA complex tightly associated to plant mitochondrial complex.
KW - Complex I
KW - Gamma carbonic anhydrase
KW - Plant mitochondria
KW - Respiratory chain
UR - http://www.scopus.com/inward/record.url?scp=20244389411&partnerID=8YFLogxK
U2 - 10.1007/s11103-004-6324-z
DO - 10.1007/s11103-004-6324-z
M3 - Article
C2 - 15821992
AN - SCOPUS:20244389411
VL - 56
SP - 947
EP - 957
JO - Plant molecular biology
JF - Plant molecular biology
SN - 0167-4412
IS - 6
ER -