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==Overview==

The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a, platform for mRNA processing factors and links gene transcription to mRNA, capping, splicing and polyadenylation. Pcf11, an essential component of, the mRNA cleavage factor IA, contains a CTD-interaction domain that binds, in a phospho-dependent manner to the heptad repeats within the RNA, polymerase II CTD. We show here that the phosphorylated CTD exists as a, dynamic disordered ensemble in solution and, by induced fit, it assumes a, structured conformation when bound to Pcf11. In addition, we detected, cis-trans populations for the CTD prolines, and found that only the, all-trans form is selected for binding. These data suggest that the, recognition of the CTD is regulated by independent site-specific, modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.

The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a platform for mRNA processing factors and links gene transcription to mRNA capping, splicing and polyadenylation. Pcf11, an essential component of the mRNA cleavage factor IA, contains a CTD-interaction domain that binds in a phospho-dependent manner to the heptad repeats within the RNA polymerase II CTD. We show here that the phosphorylated CTD exists as a dynamic disordered ensemble in solution and, by induced fit, it assumes a structured conformation when bound to Pcf11. In addition, we detected cis-trans populations for the CTD prolines, and found that only the all-trans form is selected for binding. These data suggest that the recognition of the CTD is regulated by independent site-specific modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.

==About this Structure==

Line 13:

[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Adeniran, V.E.]]

[[Category: Adeniran, V E.]]

[[Category: Hollingworth, D.]]

[[Category: Kelly, G.]]

[[Category: Martin, S.R.]]

[[Category: Martin, S R.]]

[[Category: Noble, C.G.]]

[[Category: Noble, C G.]]

[[Category: Ramos, A.]]

[[Category: Smerdon, S.J.]]

[[Category: Smerdon, S J.]]

[[Category: Taylor, I.A.]]

[[Category: Taylor, I A.]]

[[Category: CA]]

[[Category: phosphorylation]]

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[[Category: transcription]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:09 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a, platform for mRNA processing factors and links gene transcription to mRNA, capping, splicing and polyadenylation. Pcf11, an essential component of, the mRNA cleavage factor IA, contains a CTD-interaction domain that binds, in a phospho-dependent manner to the heptad repeats within the RNA, polymerase II CTD. We show here that the phosphorylated CTD exists as a, dynamic disordered ensemble in solution and, by induced fit, it assumes a, structured conformation when bound to Pcf11. In addition, we detected, cis-trans populations for the CTD prolines, and found that only the, all-trans form is selected for binding. These data suggest that the, recognition of the CTD is regulated by independent site-specific, modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.
+The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a platform for mRNA processing factors and links gene transcription to mRNA capping, splicing and polyadenylation. Pcf11, an essential component of the mRNA cleavage factor IA, contains a CTD-interaction domain that binds in a phospho-dependent manner to the heptad repeats within the RNA polymerase II CTD. We show here that the phosphorylated CTD exists as a dynamic disordered ensemble in solution and, by induced fit, it assumes a structured conformation when bound to Pcf11. In addition, we detected cis-trans populations for the CTD prolines, and found that only the all-trans form is selected for binding. These data suggest that the recognition of the CTD is regulated by independent site-specific modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Adeniran, V.E.]]
+[[Category: Adeniran, V E.]]
 [[Category: Hollingworth, D.]]
 [[Category: Kelly, G.]]
-[[Category: Martin, S.R.]]
+[[Category: Martin, S R.]]
-[[Category: Noble, C.G.]]
+[[Category: Noble, C G.]]
 [[Category: Ramos, A.]]
-[[Category: Smerdon, S.J.]]
+[[Category: Smerdon, S J.]]
-[[Category: Taylor, I.A.]]
+[[Category: Taylor, I A.]]
 [[Category: CA]]
 [[Category: phosphorylation]]
@@ Line 26: / Line 26: @@
 [[Category: transcription]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:23:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:09 2008''