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Phylogenomic analysis of Escherichia...

Anton, Brian Paul.

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Phylogenomic analysis of Escherichia coli methyltransferases and characterization of a novel subfamily of enzymes performing methyl transfer.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Phylogenomic analysis of Escherichia coli methyltransferases and characterization of a novel subfamily of enzymes performing methyl transfer./
Author:	Anton, Brian Paul.
Description:	266 p.
Notes:	Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: 1863.
Contained By:	Dissertation Abstracts International72-04B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3445689
ISBN:	9781124491400

Phylogenomic analysis of Escherichia coli methyltransferases and characterization of a novel subfamily of enzymes performing methyl transfer.
Anton, Brian Paul.

Phylogenomic analysis of Escherichia coli methyltransferases and characterization of a novel subfamily of enzymes performing methyl transfer. - 266 p.

Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: 1863.

Thesis (Ph.D.)--Boston University, 2011.

Methyltransferases, which catalyze the transfer of a methyl group from the donor S-adenosyl-L-methionine to a substrate molecule, are an ancient superfamily of enzymes comprising significant sequence and structural diversity. They are involved with nearly every conceivable biological process, having evolved to perform this same biochemical reaction on a wide variety of substrates including DNA, RNA, proteins, lipids, and small molecules. Identifying sequence-structure-function relationships within this superfamily presents considerable challenges, and this thesis comprises several computational and experimental projects directed towards that end.

ISBN: 9781124491400Subjects--Topical Terms:

1017719
Biology, Molecular.

Phylogenomic analysis of Escherichia coli methyltransferases and characterization of a novel subfamily of enzymes performing methyl transfer.
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020 $a 9781124491400
035 $a (UMI)AAI3445689
035 $a AAI3445689
040 $a UMI $c UMI
100 1 $a Anton, Brian Paul. $3 1682245
245 1 0 $a Phylogenomic analysis of Escherichia coli methyltransferases and characterization of a novel subfamily of enzymes performing methyl transfer.
300 $a 266 p.
500 $a Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: 1863.
500 $a Advisers: Richard J. Roberts; Simon Kasif.
502 $a Thesis (Ph.D.)--Boston University, 2011.
520 $a Methyltransferases, which catalyze the transfer of a methyl group from the donor S-adenosyl-L-methionine to a substrate molecule, are an ancient superfamily of enzymes comprising significant sequence and structural diversity. They are involved with nearly every conceivable biological process, having evolved to perform this same biochemical reaction on a wide variety of substrates including DNA, RNA, proteins, lipids, and small molecules. Identifying sequence-structure-function relationships within this superfamily presents considerable challenges, and this thesis comprises several computational and experimental projects directed towards that end.
520 $a We examined different types of prokaryotic methyltransferases by phylogenetic profiling and comparative genomic approaches, finding that those involved with translation exhibit relatively low rates of gene loss and horizontal change. DNA methyltransferases, by contrast, undergo frequent horizontal exchange and are not vertically inherited for long periods of time.
520 $a We found the model organism Escherichia coli K-12 encodes a total of 48 known and 14 probable methyltransferases, and we mined the literature to identify methylation activities for which the enzyme responsible was unknown. Careful comparison of these two data sets enabled predictions of the activities of many of the uncharacterized methyltransferases. We validated one of these predictions by mass spectrometry, showing that the yliG gene product (renamed RimO) modifies a universally conserved aspartic acid residue in ribosomal protein S12. This modification (--SCH3 addition) involves a radical-SAM mediated sulfur insertion as well as a methylation reaction. RimO thus belongs to a unique methyltransferase subfamily called methylthiotransferases (MTTases), and we showed phylogenetically that MTTases comprise four subclades, of which RimO orthologs form one. We predicted substrates for the two remaining uncharacterized subclades and validated one of these predictions, showing that YqeV of B. subtilis methylthiolates specific tRNA adenosine residues.
520 $a Despite acting on different substrates (protein vs. tRNA), all four MTTase sub-clades share a surprisingly high degree of sequence similarity in the predicted substrate-binding region. We used this similarity to computationally identify candidate residues involved with substrate specificity. These proteins exhibit a novel protein fold compared to other methyltransferases, and we present preliminary biochemical results that shed light on the nature of the methylation reaction carried out by RimO.
590 $a School code: 0017.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biology, Bioinformatics. $3 1018415
690 $a 0307
690 $a 0487
690 $a 0715
710 2 $a Boston University. $3 1017454
773 0 $t Dissertation Abstracts International $g 72-04B.
790 1 0 $a Roberts, Richard J., $e advisor
790 1 0 $a Kasif, Simon, $e advisor
790 $a 0017
791 $a Ph.D.
792 $a 2011
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3445689