TY - JOUR
T1 - Structural and functional characterization of annexin 1 from Medicago truncatula
AU - Kodavali, Praveen Kumar
AU - Skowronek, Krzysztof
AU - Koszela-Piotrowska, Izabela
AU - Strzelecka-Kiliszek, Agnieszka
AU - Pawlowski, Krzysztof
AU - Pikula, Slawomir
N1 - Funding Information:
This work was supported by the NODPERCEPTION contract (MRTN-CT-2006-035546) from the European Community's Marie Curie Research Training Network Program to S.P., by the grant from the Polish Ministry of Science and Higher Education N N401 140639 to A.S.-K. and by the Nencki Institute of Experimental Biology , Warsaw, Poland. Praveen Kumar Kodavali acknowledges a fellowship from the EC NODPERCEPTION contract No ESR7 .
PY - 2013/12
Y1 - 2013/12
N2 - Annexins are calcium- and membrane-binding proteins that have been shown to have diverse properties such as actin, integrin and GTP binding, both in animals and plants. Recently, Medicago truncatula annexin 1 (AnnMt1) has been suggested to participate in nodulation (Nod factor signaling) and mycorrhization in legume plants. In this report we demonstrate for the first time that recombinant AnnMt1 (rec-AnnMt1) mediates membrane permeabilization to cations with conductance ranging from 16pS to 329pS. In agreement with other structurally determined annexins, homology modeling of AnnMt1 suggests that most of the functional determinants are found on the convex surface of the modeled structure. In conclusion, we propose a potential constitutive role of AnnMt1 in Nod factor signaling as a non-specific ion channel.
AB - Annexins are calcium- and membrane-binding proteins that have been shown to have diverse properties such as actin, integrin and GTP binding, both in animals and plants. Recently, Medicago truncatula annexin 1 (AnnMt1) has been suggested to participate in nodulation (Nod factor signaling) and mycorrhization in legume plants. In this report we demonstrate for the first time that recombinant AnnMt1 (rec-AnnMt1) mediates membrane permeabilization to cations with conductance ranging from 16pS to 329pS. In agreement with other structurally determined annexins, homology modeling of AnnMt1 suggests that most of the functional determinants are found on the convex surface of the modeled structure. In conclusion, we propose a potential constitutive role of AnnMt1 in Nod factor signaling as a non-specific ion channel.
KW - Annexin 1
KW - Ion channel
KW - Medicago truncatula
KW - Protein structure
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U2 - 10.1016/j.plaphy.2013.08.010
DO - 10.1016/j.plaphy.2013.08.010
M3 - Article
C2 - 24056127
AN - SCOPUS:84884302683
SN - 0981-9428
VL - 73
SP - 56
EP - 62
JO - Plant Physiology and Biochemistry
JF - Plant Physiology and Biochemistry
ER -