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Structural and biochemical analysis ...

Silva, George H.

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Structural and biochemical analysis of the thermostable archaeal intron-encoded endonuclease I-DmoI.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structural and biochemical analysis of the thermostable archaeal intron-encoded endonuclease I-DmoI./
Author:	Silva, George H.
Description:	253 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0086.
Contained By:	Dissertation Abstracts International65-01B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3118924

Structural and biochemical analysis of the thermostable archaeal intron-encoded endonuclease I-DmoI.
Silva, George H.

Structural and biochemical analysis of the thermostable archaeal intron-encoded endonuclease I-DmoI. - 253 p.

Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0086.

Thesis (Ph.D.)--State University of New York at Albany, 2004.

Homing endonucleases are a group of enzymes encoded by mobile genetic elements. They function primarily to catalyze the mobility of their coding sequences to homologous host alleles that differ by the absence of these genes. Homing endonucleases are divided into four families based on conserved amino acid motifs: LAGLIDADG, GIY-YIG, His-Cys box and HNH. The work presented here involves I-DmoI, a thermostable archaeal intron-encoded endonuclease of the LAGLIDADG motif family.Subjects--Topical Terms:

1017719
Biology, Molecular.

Structural and biochemical analysis of the thermostable archaeal intron-encoded endonuclease I-DmoI.
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035 $a (UnM)AAI3118924
035 $a AAI3118924
040 $a UnM $c UnM
100 1 $a Silva, George H. $3 1952494
245 1 0 $a Structural and biochemical analysis of the thermostable archaeal intron-encoded endonuclease I-DmoI.
300 $a 253 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0086.
500 $a Adviser: Marlene Belfort.
502 $a Thesis (Ph.D.)--State University of New York at Albany, 2004.
520 $a Homing endonucleases are a group of enzymes encoded by mobile genetic elements. They function primarily to catalyze the mobility of their coding sequences to homologous host alleles that differ by the absence of these genes. Homing endonucleases are divided into four families based on conserved amino acid motifs: LAGLIDADG, GIY-YIG, His-Cys box and HNH. The work presented here involves I-DmoI, a thermostable archaeal intron-encoded endonuclease of the LAGLIDADG motif family.
520 $a Conditions were developed for crystallization and the structure of seleno-methionyl I-DmoI was determined to 2.2 A resolution using multi-wavelength anomalous diffraction methods. The structure was the first of a free-standing thermostable homing endonuclease with two LAGLIDADG motifs. I-DmoI shares the alphabetabetaalphabetabetaalpha subdomain fold common to this family of proteins. In all known LAGLIDADG structures, two such alpha/beta domains interact via a two-helix bundle, formed by the first alpha-helix in each domain, to generate an elongated protein with a pseudo two-fold symmetry. Each alpha-helix in the bundle is comprised of the conserved LAGLIDADG motif and functions not only in protein dimerization but also to create the active site of the endonuclease. Superposition of the structure of I-DmoI with other known LAGLIDADG protein structures was used to explore the characteristics of this protein family; specifically, (i) non-conserved residues within the catalytic core; (ii) the protein/DNA interaction of the extended beta-sheet saddle and; (iii) how the structural similarity of the alpha/beta subdomains supports the gene-duplication model for the evolution of double-motif LAGLIDADG proteins.
520 $a The nature of the LAGLIDADG two-helix bundle was investigated using a combination of bioinformatics and biochemical analyses. It was demonstrated that the LAGLIDADG helix-helix interface of I-DmoI, a double-motif monomeric protein, could be replaced with the helix-helix interface of I-CreI, a single-motif homodimer. These results were reconciled using structural and statistical analyses of the interfacial LAGLIDADG alpha-helix residues. The modular nature of the alpha/beta subdomains was explored by creating split variants of I-DmoI that were shown to form active heterodimers with wild-type cleavage specificity. A novel dimerization assay was developed to establish the extent of heterodimer formation in order to determine cleavage activity relative to wild-type I-DmoI. Taken together, these results allowed us to speculate on the evolution of LAGLIDADG homing endonucleases.
590 $a School code: 0668.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, General. $3 1019105
650 4 $a Biology, Genetics. $3 1017730
690 $a 0307
690 $a 0786
690 $a 0369
710 2 0 $a State University of New York at Albany. $3 769258
773 0 $t Dissertation Abstracts International $g 65-01B.
790 1 0 $a Belfort, Marlene, $e advisor
790 $a 0668
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3118924