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Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
Aquaporins are membrane proteins that facilitate water transport across the membranes in various microorganisms, plants and animals. Plant aquaporins are divided into four groups based on the amino acid sequence similarities and intracellular localization; plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), nodulin-like intrinsic proteins (NIPs) and small basic intrinsic proteins (SIPs). We found 35 EST sequences homologous to 3’ and 5’ termini of the partial cDNA of P. nil in the GenBank NCBl database. cDNA encoding full length aquaporin of P. nil was cloned with the use of the reverse transcription-polymerase chain reaction (RT-PCR). The 1189 bp full length cDNA sequence of aquaporin P. nil {PnPIPl} was obtained. Analysis of protein hydropathy indicated that cloned part of PnPIPl contained the NPA motif (Asn-Pro-Ala) that is present in all known aquaporins. The amino acid sequence of the PnPIPl protein exhibits 90, 89 and 88% sequence similarity to Petunio x hybrida, Nicotiana excelior and Fraxinus excelsior aquaporins respectively. We showed that the EST database is a useful tool for identification of the complete cDNA of known genes.
Biotechnologia, vol.81, 2 (2008)-.
0860-7796 ; oai:rcin.org.pl:73917 ; IChB B-76
Library of Institute of Bioorganic Chemistry PAS
Creative Commons Attribution BY-SA 4.0 license
Institute of Bioorganic Chemistry of the Polish Academy of Science
Institute of Bioorganic Chemistry of the Polish Academy of Science
Oct 2, 2020
Jun 27, 2019
363
https://rcin.org.pl./publication/96756
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