2oyt: Difference between revisions

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==Overview==

The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bases in, the genome using an extrahelical base recognition mechanism. Efficient, removal of uracil is essential for prevention of C-to-T transition, mutations arising from cytosine deamination, cytotoxic U*A pairs arising, from incorporation of dUTP in DNA, and for increasing immunoglobulin gene, diversity during the acquired immune response. A central event in all of, these UNG-mediated processes is the singling out of rare U*A or U*G base, pairs in a background of approximately 10(9) T*A or C*G base pairs in the, human genome. Here we establish for the human and Escherichia coli enzymes, that discrimination of thymine and uracil is initiated by thermally, induced opening of T*A and U*A base pairs and not by active participation, of the enzyme. Thus, base-pair dynamics has a critical role in the, genome-wide search for uracil, and may be involved in initial damage, recognition by other DNA repair glycosylases.

The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bases in the genome using an extrahelical base recognition mechanism. Efficient removal of uracil is essential for prevention of C-to-T transition mutations arising from cytosine deamination, cytotoxic U*A pairs arising from incorporation of dUTP in DNA, and for increasing immunoglobulin gene diversity during the acquired immune response. A central event in all of these UNG-mediated processes is the singling out of rare U*A or U*G base pairs in a background of approximately 10(9) T*A or C*G base pairs in the human genome. Here we establish for the human and Escherichia coli enzymes that discrimination of thymine and uracil is initiated by thermally induced opening of T*A and U*A base pairs and not by active participation of the enzyme. Thus, base-pair dynamics has a critical role in the genome-wide search for uracil, and may be involved in initial damage recognition by other DNA repair glycosylases.

==Disease==

Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191525 191525]]

==About this Structure==

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Line 16:

[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Amzel, L.M.]]

[[Category: Amzel, L M.]]

[[Category: Bianchet, M.A.]]

[[Category: Bianchet, M A.]]

[[Category: D.J., Krosky.]]

[[Category: D J., Krosky.]]

[[Category: Stivers, J.T]]

[[Category: Stivers, J T]]

[[Category: enzyme-dna complex]]

[[Category: hydrolase/dna complex]]

[[Category: ung2]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bases in, the genome using an extrahelical base recognition mechanism. Efficient, removal of uracil is essential for prevention of C-to-T transition, mutations arising from cytosine deamination, cytotoxic U*A pairs arising, from incorporation of dUTP in DNA, and for increasing immunoglobulin gene, diversity during the acquired immune response. A central event in all of, these UNG-mediated processes is the singling out of rare U*A or U*G base, pairs in a background of approximately 10(9) T*A or C*G base pairs in the, human genome. Here we establish for the human and Escherichia coli enzymes, that discrimination of thymine and uracil is initiated by thermally, induced opening of T*A and U*A base pairs and not by active participation, of the enzyme. Thus, base-pair dynamics has a critical role in the, genome-wide search for uracil, and may be involved in initial damage, recognition by other DNA repair glycosylases.
+The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bases in the genome using an extrahelical base recognition mechanism. Efficient removal of uracil is essential for prevention of C-to-T transition mutations arising from cytosine deamination, cytotoxic U*A pairs arising from incorporation of dUTP in DNA, and for increasing immunoglobulin gene diversity during the acquired immune response. A central event in all of these UNG-mediated processes is the singling out of rare U*A or U*G base pairs in a background of approximately 10(9) T*A or C*G base pairs in the human genome. Here we establish for the human and Escherichia coli enzymes that discrimination of thymine and uracil is initiated by thermally induced opening of T*A and U*A base pairs and not by active participation of the enzyme. Thus, base-pair dynamics has a critical role in the genome-wide search for uracil, and may be involved in initial damage recognition by other DNA repair glycosylases.
+==Disease==
+Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191525 191525]]
 ==About this Structure==
@@ Line 13: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Amzel, L.M.]]
+[[Category: Amzel, L M.]]
-[[Category: Bianchet, M.A.]]
+[[Category: Bianchet, M A.]]
-[[Category: D.J., Krosky.]]
+[[Category: D J., Krosky.]]
-[[Category: Stivers, J.T]]
+[[Category: Stivers, J T]]
 [[Category: enzyme-dna complex]]
 [[Category: hydrolase/dna complex]]
 [[Category: ung2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:36:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:02 2008''