Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization

The efficient uptake is important for the xylose utilization by Saccharomyces cerevisiae. A heterogenous transporter Mgt05196p was cloned from Meyerozyma guilliermondii and expressed in Saccharomyces cerevisiae [1]. This data article contains the transport characteristics of Mgt05196p in S. cerevisi...

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Main Authors: Chengqiang Wang, Xiaoming Bao, Yanwei Li, Chunlei Jiao, Jin Hou, Qingzhu Zhang, Weixin Zhang, Weifeng Liu, Yu Shen
Format: Article
Language:English
Published: Elsevier 2015-09-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340915000736
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author Chengqiang Wang
Xiaoming Bao
Yanwei Li
Chunlei Jiao
Jin Hou
Qingzhu Zhang
Weixin Zhang
Weifeng Liu
Yu Shen
author_facet Chengqiang Wang
Xiaoming Bao
Yanwei Li
Chunlei Jiao
Jin Hou
Qingzhu Zhang
Weixin Zhang
Weifeng Liu
Yu Shen
author_sort Chengqiang Wang
collection DOAJ
description The efficient uptake is important for the xylose utilization by Saccharomyces cerevisiae. A heterogenous transporter Mgt05196p was cloned from Meyerozyma guilliermondii and expressed in Saccharomyces cerevisiae [1]. This data article contains the transport characteristics of Mgt05196p in S. cerevisiae. The fluorescence of fusion protein Mgt05196p-GFP expressing strain was located on the cell surface demonstrated that the heterogenous transporter Mgt05196p was targeted to the plasma membrane of S. cerevisiae. The expressing of Mgt05196p in the hxt null S. cerevisiae endowed the strain with the glucose and d-xylose absorption capacity, as well as expressing the native d-xylose transporter Gal2p. The transmembrane domains of Mgt05196p were predicted and compared with the XylEp, whose crystal structure was revealed. And then, the homologous modeling of Mgt05196p was built basing on the XylEp to find out the crucial amino acid residues for sugars binding and transport.
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spelling doaj.art-b7eb6f67572c493b9d95074a74b36c722022-12-22T00:53:48ZengElsevierData in Brief2352-34092015-09-014C11912610.1016/j.dib.2015.05.005Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilizationChengqiang Wang0Xiaoming Bao1Yanwei Li2Chunlei Jiao3Jin Hou4Qingzhu Zhang5Weixin Zhang6Weifeng Liu7Yu Shen8The State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaThe State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaEnvironment Research Institute, Shandong University, Shan Da Nan Road 27, Jinan 250100, PR ChinaThe State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaThe State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaEnvironment Research Institute, Shandong University, Shan Da Nan Road 27, Jinan 250100, PR ChinaThe State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaThe State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaThe State Key Laboratory of Microbial Technology, Shandong University, Shan Da Nan Road27, Jinan 250100, PR ChinaThe efficient uptake is important for the xylose utilization by Saccharomyces cerevisiae. A heterogenous transporter Mgt05196p was cloned from Meyerozyma guilliermondii and expressed in Saccharomyces cerevisiae [1]. This data article contains the transport characteristics of Mgt05196p in S. cerevisiae. The fluorescence of fusion protein Mgt05196p-GFP expressing strain was located on the cell surface demonstrated that the heterogenous transporter Mgt05196p was targeted to the plasma membrane of S. cerevisiae. The expressing of Mgt05196p in the hxt null S. cerevisiae endowed the strain with the glucose and d-xylose absorption capacity, as well as expressing the native d-xylose transporter Gal2p. The transmembrane domains of Mgt05196p were predicted and compared with the XylEp, whose crystal structure was revealed. And then, the homologous modeling of Mgt05196p was built basing on the XylEp to find out the crucial amino acid residues for sugars binding and transport.http://www.sciencedirect.com/science/article/pii/S2352340915000736
spellingShingle Chengqiang Wang
Xiaoming Bao
Yanwei Li
Chunlei Jiao
Jin Hou
Qingzhu Zhang
Weixin Zhang
Weifeng Liu
Yu Shen
Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization
Data in Brief
title Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization
title_full Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization
title_fullStr Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization
title_full_unstemmed Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization
title_short Data set for cloning and characterization of heterologous transporters in Saccharomyces cerevisiae and identification of important amino acids for xylose utilization
title_sort data set for cloning and characterization of heterologous transporters in saccharomyces cerevisiae and identification of important amino acids for xylose utilization
url http://www.sciencedirect.com/science/article/pii/S2352340915000736
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