TY - JOUR
T1 - Characterization of substrate specificity of a rice silicon transporter, Lsi1
AU - Mitani, Namiki
AU - Yamaji, Naoki
AU - Ma, Jian Feng
N1 - Funding Information:
This research was supported by a grant-in-aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan (nos. 15380053 and 17078008 to J.F.M.) and a grant from the Ministry of Agriculture, Forestry and Fisheries of Japan (Rice Genome Project IP-5003 to J.F.M.). We thank Dr. Maki Katsuhara and Dr. Nobuyuki Uozumi for instruction in oocyte assay. We also thank Fang Jie Zhao for his critical reading of this paper.
PY - 2008/7
Y1 - 2008/7
N2 - Lsi1 (OsNIP2;1) is the first silicon (silicic acid) transporter identified in plant, which belongs to the nodulin 26-like intrinsic membrane protein (NIP) subfamily. In this study, we characterized the function of this transporter by using the Xenopus laevis oocyte expression system. The transport activity of Lsi1 for silicic acid was significantly inhibited by HgCl2 but not by low temperature. Lsi1 also showed an efflux transport activity for silicic acid. The substrate specificity study showed that Lsi1 was able to transport urea and boric acid; however, the transport activity for silicic acid was not affected by the presence of equimolar urea and was decreased only slightly by boric acid. Furthermore, among the NIPs subgroup, OsNIP2;2 showed transport activity for silicic acid, whereas OsNIP1;1 and OsNIP3;1 did not. We propose that Lsi1 and its close homologues form a unique subgroup of NIP with a distinct ar/R selectivity filter, which is located in the narrowest region on the extra-membrane mouth and govern the substrate specificity of the pore.
AB - Lsi1 (OsNIP2;1) is the first silicon (silicic acid) transporter identified in plant, which belongs to the nodulin 26-like intrinsic membrane protein (NIP) subfamily. In this study, we characterized the function of this transporter by using the Xenopus laevis oocyte expression system. The transport activity of Lsi1 for silicic acid was significantly inhibited by HgCl2 but not by low temperature. Lsi1 also showed an efflux transport activity for silicic acid. The substrate specificity study showed that Lsi1 was able to transport urea and boric acid; however, the transport activity for silicic acid was not affected by the presence of equimolar urea and was decreased only slightly by boric acid. Furthermore, among the NIPs subgroup, OsNIP2;2 showed transport activity for silicic acid, whereas OsNIP1;1 and OsNIP3;1 did not. We propose that Lsi1 and its close homologues form a unique subgroup of NIP with a distinct ar/R selectivity filter, which is located in the narrowest region on the extra-membrane mouth and govern the substrate specificity of the pore.
KW - Aquaporin
KW - NIP subfamily
KW - Phosphorylation
KW - Rice
KW - Silicon
KW - Substrate specificity
KW - ar/R selectivity filter
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U2 - 10.1007/s00424-007-0408-y
DO - 10.1007/s00424-007-0408-y
M3 - Review article
C2 - 18214526
AN - SCOPUS:43749100033
SN - 0031-6768
VL - 456
SP - 679
EP - 686
JO - Pflugers Archiv fur die gesamte Physiologie des Menschen und der Tiere
JF - Pflugers Archiv fur die gesamte Physiologie des Menschen und der Tiere
IS - 4
ER -