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Mutations in NPr/HPr affecting phosp...

University of California, San Diego.

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Mutations in NPr/HPr affecting phosphoryl transfer in the phosphotransferase system of Escherichia coli.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Mutations in NPr/HPr affecting phosphoryl transfer in the phosphotransferase system of Escherichia coli./
作者:	Rettner, Rachael Elizabeth.
面頁冊數:	55 p.
附註:	Adviser: Milton H. Saier.
Contained By:	Masters Abstracts International47-01.
標題:	Biology, Bioinformatics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1456305
ISBN:	9780549694267

Mutations in NPr/HPr affecting phosphoryl transfer in the phosphotransferase system of Escherichia coli.
Rettner, Rachael Elizabeth.

Mutations in NPr/HPr affecting phosphoryl transfer in the phosphotransferase system of Escherichia coli. - 55 p.

Adviser: Milton H. Saier.

Thesis (M.S.)--University of California, San Diego, 2008.

Protein evolution studies can provide key insight into the structure-function relationship of specific proteins. This project focuses on two proteins involved in the phosphotransferase system (PTS) of E. coli, which is a system used by bacteria to take up various sugars. Within this system, HPr functions to allow the uptake of the sugar mannitol, while NPr is involved in the regulation of nitrogen metabolism. Although these proteins are homologous, there is little cross reactivity. This project attempts to mutate NPr so that it takes on the function of HPr using both bioinformatic and protein engineering experiments.

ISBN: 9780549694267Subjects--Topical Terms:

1018415
Biology, Bioinformatics.

Mutations in NPr/HPr affecting phosphoryl transfer in the phosphotransferase system of Escherichia coli.
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245 1 0 $a Mutations in NPr/HPr affecting phosphoryl transfer in the phosphotransferase system of Escherichia coli.
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502 $a Thesis (M.S.)--University of California, San Diego, 2008.
520 $a Protein evolution studies can provide key insight into the structure-function relationship of specific proteins. This project focuses on two proteins involved in the phosphotransferase system (PTS) of E. coli, which is a system used by bacteria to take up various sugars. Within this system, HPr functions to allow the uptake of the sugar mannitol, while NPr is involved in the regulation of nitrogen metabolism. Although these proteins are homologous, there is little cross reactivity. This project attempts to mutate NPr so that it takes on the function of HPr using both bioinformatic and protein engineering experiments.
520 $a Bioinformatic analysis revealed two consensus sequences within HPr and NPr. HPr contains a C-terminal "PN" and a N-terminal "QT," while NPr contains a C-terminal "NK" and a N-terminal "LMML." Site-specific mutagenesis was used to mutate 14 residues in NPr to match those of HPr, including residues of the consensus sequence. Electroporation of this chimeric gene into cells lacking HPr and FPr (2Delta cells) allowed the cells to grow on mannitol, showing that the specific mutations caused NPr to take on HPr function. Growth experiments on glucose, mannitol, mannose, glucosamine, and N-acetyl glucosamine revealed that the Chimera protein allows uptake of all these sugars. Furthermore, 2Delta cells with the chimera gene grew slightly better on mannose and glucosamine than 2Delta cells with the HPr gene. Finally, NPr genes with fewer mutations did not allow 2Delta cells to grow efficiently on mannitol, suggesting that most of the 14 originally identified residues are necessary for HPr function.
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