A LEA model peptide protects the function of a red fluorescent protein in the dry state
We tested whether a short model peptide derived from a group 3 late embryogenesis abundant (G3LEA) protein is able to maintain the fluorescence activity of a red fluorescent protein, mKate2, in the dry state. The fluorescence intensity of mKate2 alone decreased gradually through repeated dehydration...
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doaj-94939aa212ce4eb99dd024ac22398a892020-11-24T21:56:48ZengElsevierBiochemistry and Biophysics Reports2405-58082019-03-01172731A LEA model peptide protects the function of a red fluorescent protein in the dry stateTakao Furuki0Tatsuya Niwa1Hideki Taguchi2Rie Hatanaka3Takahiro Kikawada4Minoru Sakurai5Center for Biological Resources and Informatics, Tokyo Institute of Technology, B-62 4259, Nagatsuta-cho, Midori-ku, Yokohama 226-8501, JapanCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology S2-19, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, JapanCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology S2-19, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, JapanMolecular Biomimetics Research Unit, Division of Biotechnology, Institute of Agrobiological Sciences, National Institute of Agriculture and Food Research Organization, Ohwashi 1-2, Tsukuba 305-8634, JapanMolecular Biomimetics Research Unit, Division of Biotechnology, Institute of Agrobiological Sciences, National Institute of Agriculture and Food Research Organization, Ohwashi 1-2, Tsukuba 305-8634, JapanCenter for Biological Resources and Informatics, Tokyo Institute of Technology, B-62 4259, Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan; Corresponding author.We tested whether a short model peptide derived from a group 3 late embryogenesis abundant (G3LEA) protein is able to maintain the fluorescence activity of a red fluorescent protein, mKate2, in the dry state. The fluorescence intensity of mKate2 alone decreased gradually through repeated dehydration-rehydration treatments. However, in the presence of the LEA model peptide, the peak intensity was maintained almost perfectly during such stress treatments, which implies that the three dimensional structure of the active site of mKate2 was protected even under severe desiccation conditions. For comparison, similar experiments were performed with other additives such as a native G3LEA protein, trehalose and BSA, all of whose protective abilities were lower than that of the LEA model peptide. Keywords: LEA protein, Anhydrobiosis, Trehalose, Desiccation tolerance, Dry preservationhttp://www.sciencedirect.com/science/article/pii/S2405580818302085 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Takao Furuki Tatsuya Niwa Hideki Taguchi Rie Hatanaka Takahiro Kikawada Minoru Sakurai |
spellingShingle |
Takao Furuki Tatsuya Niwa Hideki Taguchi Rie Hatanaka Takahiro Kikawada Minoru Sakurai A LEA model peptide protects the function of a red fluorescent protein in the dry state Biochemistry and Biophysics Reports |
author_facet |
Takao Furuki Tatsuya Niwa Hideki Taguchi Rie Hatanaka Takahiro Kikawada Minoru Sakurai |
author_sort |
Takao Furuki |
title |
A LEA model peptide protects the function of a red fluorescent protein in the dry state |
title_short |
A LEA model peptide protects the function of a red fluorescent protein in the dry state |
title_full |
A LEA model peptide protects the function of a red fluorescent protein in the dry state |
title_fullStr |
A LEA model peptide protects the function of a red fluorescent protein in the dry state |
title_full_unstemmed |
A LEA model peptide protects the function of a red fluorescent protein in the dry state |
title_sort |
lea model peptide protects the function of a red fluorescent protein in the dry state |
publisher |
Elsevier |
series |
Biochemistry and Biophysics Reports |
issn |
2405-5808 |
publishDate |
2019-03-01 |
description |
We tested whether a short model peptide derived from a group 3 late embryogenesis abundant (G3LEA) protein is able to maintain the fluorescence activity of a red fluorescent protein, mKate2, in the dry state. The fluorescence intensity of mKate2 alone decreased gradually through repeated dehydration-rehydration treatments. However, in the presence of the LEA model peptide, the peak intensity was maintained almost perfectly during such stress treatments, which implies that the three dimensional structure of the active site of mKate2 was protected even under severe desiccation conditions. For comparison, similar experiments were performed with other additives such as a native G3LEA protein, trehalose and BSA, all of whose protective abilities were lower than that of the LEA model peptide. Keywords: LEA protein, Anhydrobiosis, Trehalose, Desiccation tolerance, Dry preservation |
url |
http://www.sciencedirect.com/science/article/pii/S2405580818302085 |
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