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[ subject:"Chemistry, Biochemistry." ]
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Characterization of bacterial homing...
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Characterization of bacterial homing endonuclease I-Ssp6803I.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Characterization of bacterial homing endonuclease I-Ssp6803I./
作者:
Zhao, Lei.
面頁冊數:
127 p.
附註:
Adviser: Barry L. Stoddard.
Contained By:
Dissertation Abstracts International69-06B.
標題:
Chemistry, Biochemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3318475
ISBN:
9780549678267
Characterization of bacterial homing endonuclease I-Ssp6803I.
Zhao, Lei.
Characterization of bacterial homing endonuclease I-Ssp6803I.
- 127 p.
Adviser: Barry L. Stoddard.
Thesis (Ph.D.)--University of Washington, 2008.
The homing endonuclease I-Ssp6803I causes the insertion and persistence of a group I self-splicing intron into the anticodon loop of the tRNA fMet gene in the cyanobacteria Synechocystis PCC6803. This enzyme and its host intron represent the only known combination of a persistent intron and associated homing endonuclease within bacterial tRNA genes. In this study, we predicted that this enzyme, which is dissimilar to other known homing endonucleases, might contain the PD-(D/E)XK nuclease catalytic motif---a fold normally associated with bacterial restriction endonucleases. This prediction, combined with a mutational screen for catalytically inactivating point mutations, allowed us to express, solubilize and crystallize I-Ssp6803I in complex with its target DNA. The 3.1A crystal structure of the protein-DNA complex confirmed the presence of the PD(D/E)XK motif and also revealed the use of a unique tetrameric assembly to promote recognition of a single long target site. The binding specificity profile of I-Ssp6803I was then determined by measuring the effect of every possible base substitution across its 23-basepair target site. The endonuclease displays relatively low binding specificity, corresponding to a profile reflects sequence constraints on its host tRNAfMet gene.
ISBN: 9780549678267Subjects--Topical Terms:
1017722
Chemistry, Biochemistry.
Characterization of bacterial homing endonuclease I-Ssp6803I.
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The homing endonuclease I-Ssp6803I causes the insertion and persistence of a group I self-splicing intron into the anticodon loop of the tRNA fMet gene in the cyanobacteria Synechocystis PCC6803. This enzyme and its host intron represent the only known combination of a persistent intron and associated homing endonuclease within bacterial tRNA genes. In this study, we predicted that this enzyme, which is dissimilar to other known homing endonucleases, might contain the PD-(D/E)XK nuclease catalytic motif---a fold normally associated with bacterial restriction endonucleases. This prediction, combined with a mutational screen for catalytically inactivating point mutations, allowed us to express, solubilize and crystallize I-Ssp6803I in complex with its target DNA. The 3.1A crystal structure of the protein-DNA complex confirmed the presence of the PD(D/E)XK motif and also revealed the use of a unique tetrameric assembly to promote recognition of a single long target site. The binding specificity profile of I-Ssp6803I was then determined by measuring the effect of every possible base substitution across its 23-basepair target site. The endonuclease displays relatively low binding specificity, corresponding to a profile reflects sequence constraints on its host tRNAfMet gene.
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