2es6: Difference between revisions

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==Overview==

Although the abundant sterile alpha motif (SAM) domain was originally, classified as a protein-protein interaction domain, it has recently been, shown that certain SAM domains have the ability to bind RNA, defining a, new type of post-transcriptional gene regulator. To further understand the, function of SAM-RNA recognition, we determined the solution structures of, the SAM domain of the Saccharomyces cerevisiae Vts1p (Vts1p-SAM) and the, Smaug response element (SRE) stem-loop RNA as a complex and in isolation., The structures show that Vts1p-SAM recognizes predominantly the shape of, the SRE rather than its sequence, with the exception of a G located at the, tip of the pentaloop. Using microarray gene profiling, we identified, several genes in S. cerevisiae that seem to be regulated by Vts1p and, contain one or more copies of the SRE.

Although the abundant sterile alpha motif (SAM) domain was originally classified as a protein-protein interaction domain, it has recently been shown that certain SAM domains have the ability to bind RNA, defining a new type of post-transcriptional gene regulator. To further understand the function of SAM-RNA recognition, we determined the solution structures of the SAM domain of the Saccharomyces cerevisiae Vts1p (Vts1p-SAM) and the Smaug response element (SRE) stem-loop RNA as a complex and in isolation. The structures show that Vts1p-SAM recognizes predominantly the shape of the SRE rather than its sequence, with the exception of a G located at the tip of the pentaloop. Using microarray gene profiling, we identified several genes in S. cerevisiae that seem to be regulated by Vts1p and contain one or more copies of the SRE.

==About this Structure==

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[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Allain, F.H.T.]]

[[Category: Allain, F H.T.]]

[[Category: gene regulation]]

[[Category: protein structure]]

[[Category: sam domain]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Although the abundant sterile alpha motif (SAM) domain was originally, classified as a protein-protein interaction domain, it has recently been, shown that certain SAM domains have the ability to bind RNA, defining a, new type of post-transcriptional gene regulator. To further understand the, function of SAM-RNA recognition, we determined the solution structures of, the SAM domain of the Saccharomyces cerevisiae Vts1p (Vts1p-SAM) and the, Smaug response element (SRE) stem-loop RNA as a complex and in isolation., The structures show that Vts1p-SAM recognizes predominantly the shape of, the SRE rather than its sequence, with the exception of a G located at the, tip of the pentaloop. Using microarray gene profiling, we identified, several genes in S. cerevisiae that seem to be regulated by Vts1p and, contain one or more copies of the SRE.
+Although the abundant sterile alpha motif (SAM) domain was originally classified as a protein-protein interaction domain, it has recently been shown that certain SAM domains have the ability to bind RNA, defining a new type of post-transcriptional gene regulator. To further understand the function of SAM-RNA recognition, we determined the solution structures of the SAM domain of the Saccharomyces cerevisiae Vts1p (Vts1p-SAM) and the Smaug response element (SRE) stem-loop RNA as a complex and in isolation. The structures show that Vts1p-SAM recognizes predominantly the shape of the SRE rather than its sequence, with the exception of a G located at the tip of the pentaloop. Using microarray gene profiling, we identified several genes in S. cerevisiae that seem to be regulated by Vts1p and contain one or more copies of the SRE.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Allain, F.H.T.]]
+[[Category: Allain, F H.T.]]
 [[Category: gene regulation]]
 [[Category: protein structure]]
 [[Category: sam domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:31:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:01 2008''