Structure and function of cGMP-dependent protein kinases

2005 ◽  
pp. 105-149 ◽  
Author(s):  
A. Pfeifer ◽  
P. Ruth ◽  
W. Dostmann ◽  
M. Sausbier ◽  
P. Klatt ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Structure And Function ◽  
Dependent Protein ◽  
And Function

The Relationship between Structure and Function in AMP-dependent Protein Kinases

1986 ◽  
Vol 478 (1 Metabolic Reg) ◽  
pp. 191-202 ◽  
Author(s):  
SUSAN S. TAYLOR ◽  
LAKSHMI D. SARASWAT ◽  
JEAN A. TONER ◽  
JOSÉ BUBIS
Keyword(s):  
Protein Kinases ◽  
Structure And Function ◽  
Dependent Protein ◽  
And Function ◽  
The Relationship

Relation Between Structure and Function in cAMP-Dependent Protein Kinases

1988 ◽  
pp. 327-341
Author(s):  
Susan S. Taylor ◽  
José Bubis ◽  
Janusz Sowadski ◽  
Jean A. Toner ◽  
Lakshmi D. Saraswat
Keyword(s):  
Protein Kinases ◽  
Structure And Function ◽  
Dependent Protein ◽  
And Function

Overview of the Structure and Function of Protein Kinases

2017 ◽  
Vol 13 (2) ◽  
Author(s):  
Sugunadevi Sakkiah ◽  
Guang Ping Cao ◽  
Staya P. Gupta ◽  
Keun Woo Lee
Keyword(s):  
Protein Kinases ◽  
Structure And Function ◽  
And Function

scholarly journals Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

2006 ◽  
Vol 17 (4) ◽  
pp. 1744-1757 ◽  
Author(s):  
Astrid S. Clarke ◽  
Eva Samal ◽  
Lorraine Pillus
Keyword(s):  
Rna Polymerase Ii ◽  
Transcriptional Activation ◽  
Structural Changes ◽  
Structure And Function ◽  
Pol Ii ◽  
Dependent Protein ◽  
Nucleolar Chromatin ◽  
Essential Function ◽  
And Function ◽  
Protein Deacetylase

Among acetyltransferases, the MYST family enzyme Esa1p is distinguished for its essential function and contribution to transcriptional activation and DNA double-stranded break repair. Here we report that Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA) of the nucleolus. These effects are mediated through Esa1p's HAT activity and correlate with changes within the nucleolus. Esa1p is enriched within the rDNA, as is the NAD-dependent protein deacetylase Sir2p, and the acetylation levels of key Esa1p histone targets are reduced in the rDNA in esa1 mutants. Although mutants of both ESA1 and SIR2 have enhanced rates of rDNA recombination, esa1 effects are more modest yet result in distinct structural changes of rDNA chromatin. Surprisingly, increased expression of ESA1 can bypass the requirement for Sir2p in rDNA silencing, suggesting that these two enzymes with seemingly opposing activities both contribute to achieve optimal nucleolar chromatin structure and function.

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