INVESTIGADORES
ZABALETA Eduardo Julian
congresos y reuniones científicas
Título:
INTERACTION STUDIES BETWEEN FIVE MITOCHONDRIAL -CARBONIC ANDHYDRASES FROM ARABIDOPSIS THALIANA
Autor/es:
MARTIN, M. V.; VILLARREAL, F.; EDUARDO JULIAN ZABALETA
Lugar:
Pinamar
Reunión:
Congreso; PABMB 10th congress; 2005
Resumen:
A novel group of 5 ¥ã-Carbonic anhydrases (¥ã- CA1, ¥ã- CA2, ¥ã-
CA3, ¥ã- CAL1 y ¥ã- CAL2), has been recently identified in¥ã-Carbonic anhydrases (¥ã- CA1, ¥ã- CA2, ¥ã-
CA3, ¥ã- CAL1 y ¥ã- CAL2), has been recently identified in¥ã- CAL1 y ¥ã- CAL2), has been recently identified in
Arabidopsis thaliana. These proteins are targeted to mitochondria,
and they are specifically located bounded mainly to the Complex I
(NADH-ubiquinone oxidorreductase) of the mitochondrial electron
transport chain. The ¥ã-Carbonic anhydrase proteins containing lefthanded
parallel beta helix (L©¬H) domain display imperfect tandem
repeated copies of hexapeptide sequence characterized as [LIV]-
[GAED]-X2-[STAV]-X. This domain is involved in protein-protein
interaction. There is only one example fully characterized of ¥ã- CA
from Methanosarcina thermophila, named CAM. Cristallografic
studies of this protein shown a quaternary homotrimeric structure
coordinating a Zinc ion. In the present work we postulate a plant
CA complex by in vivo Yeast two hybrid assays.. These proteins are targeted to mitochondria,
and they are specifically located bounded mainly to the Complex I
(NADH-ubiquinone oxidorreductase) of the mitochondrial electron
transport chain. The ¥ã-Carbonic anhydrase proteins containing lefthanded
parallel beta helix (L©¬H) domain display imperfect tandem
repeated copies of hexapeptide sequence characterized as [LIV]-
[GAED]-X2-[STAV]-X. This domain is involved in protein-protein
interaction. There is only one example fully characterized of ¥ã- CA
from Methanosarcina thermophila, named CAM. Cristallografic
studies of this protein shown a quaternary homotrimeric structure
coordinating a Zinc ion. In the present work we postulate a plant
CA complex by in vivo Yeast two hybrid assays.¥ã-Carbonic anhydrase proteins containing lefthanded
parallel beta helix (L©¬H) domain display imperfect tandem
repeated copies of hexapeptide sequence characterized as [LIV]-
[GAED]-X2-[STAV]-X. This domain is involved in protein-protein
interaction. There is only one example fully characterized of ¥ã- CA
from Methanosarcina thermophila, named CAM. Cristallografic
studies of this protein shown a quaternary homotrimeric structure
coordinating a Zinc ion. In the present work we postulate a plant
CA complex by in vivo Yeast two hybrid assays.¥ã- CA
from Methanosarcina thermophila, named CAM. Cristallografic
studies of this protein shown a quaternary homotrimeric structure
coordinating a Zinc ion. In the present work we postulate a plant
CA complex by in vivo Yeast two hybrid assays.Methanosarcina thermophila, named CAM. Cristallografic
studies of this protein shown a quaternary homotrimeric structure
coordinating a Zinc ion. In the present work we postulate a plant
CA complex by in vivo Yeast two hybrid assays.in vivo Yeast two hybrid assays.