scholarly journals The Carboxyl-terminal Region of the Retinoblastoma Protein Binds Non-competitively to Protein Phosphatase Type 1α and Inhibits Catalytic Activity

2000 ◽  
Vol 275 (36) ◽  
pp. 27784-27789 ◽  
Author(s):  
Sama Tamrakar ◽  
John W. Ludlow
Keyword(s):  
Catalytic Activity ◽  
Protein Phosphatase ◽  
Retinoblastoma Protein ◽  
Terminal Region ◽  
Carboxyl Terminal ◽  
Protein Phosphatase Type

scholarly journals Binding of select forms of pRB to protein phosphatase type 1 independent of catalytic activity

Oncogene ◽  
1999 ◽  
Vol 18 (54) ◽  
pp. 7803-7809 ◽  
Author(s):  
Sama Tamrakar ◽  
Sibylle Mittnacht ◽  
John W Ludlow
Keyword(s):  
Catalytic Activity ◽  
Protein Phosphatase ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

The Effects of Mutations in the Carboxyl-Terminal Region on the Catalytic Activity of Escherichia coli Signal Peptidase I

2007 ◽  
Vol 143 (2) ◽  
pp. 237-242
Author(s):  
Y.-T. Kim ◽  
H. Yoshida ◽  
M. Kojima ◽  
R. Kurita ◽  
W. Nishii ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Terminal Region ◽  
Signal Peptidase ◽  
Signal Peptidase I ◽  
Carboxyl Terminal

The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability

2012 ◽  
Vol 40 (6) ◽  
pp. 477-486.e1 ◽  
Author(s):  
Senkottuvelan Kadirvel ◽  
Kazumichi Furuyama ◽  
Hideo Harigae ◽  
Kiriko Kaneko ◽  
Yoshiko Tamai ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Protein Stability ◽  
Terminal Region ◽  
Aminolevulinate Synthase ◽  
Carboxyl Terminal

scholarly journals The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit.

1993 ◽  
Vol 7 (4) ◽  
pp. 555-569 ◽  
Author(s):  
T Durfee ◽  
K Becherer ◽  
P L Chen ◽  
S H Yeh ◽  
Y Yang ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Retinoblastoma Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Overexpression of SIS2, which contains an extremely acidic region, increases the expression of SWI4, CLN1 and CLN2 in sit4 mutants.

Genetics ◽  
1995 ◽  
Vol 139 (1) ◽  
pp. 95-107 ◽  
Author(s):  
C J Di Como ◽  
R Bose ◽  
K T Arndt
Keyword(s):  
Growth Rate ◽  
Protein Phosphatase ◽  
Rnase A ◽  
Micrococcal Nuclease ◽  
Nuclear Fraction ◽  
High Copy Number Plasmid ◽  
Carboxyl Terminal ◽  
Rna Accumulation ◽  
Bud Initiation ◽  
Acidic Region

Abstract The Saccharomyces cerevisiae SIS2 gene was identified by its ability, when present on a high copy number plasmid, to increase dramatically the growth rate of sit4 mutants. SIT4 encodes a type 2A-related protein phosphatase that is required in late G1 for normal G1 cyclin expression and for bud initiation. Overexpression of SIS2, which contains an extremely acidic carboxyl terminal region, stimulated the rate of CLN1, CLN2, SWI4 and CLB5 expression in sit4 mutants. Also, overexpression of SIS2 in a CLN1 cln2 cln3 strain stimulated the growth rate and the rate of CLN1 and CLB5 RNA accumulation during late G1. The SIS2 protein fractionated with nuclei and was released from the nuclear fraction by treatment with either DNase I or micrococcal nuclease, but not by RNase A. This result, combined with the finding that overexpression of SIS2 is extremely to a strain containing lower than normal levels of histones H2A and H2B, suggests that SIS2 might function to stimulate transcription via an interaction with chromatin.

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