scholarly journals Crystal Structure of the Complex between the Catalytic Subunit of Serine/Threonine Protein Phosphatase 1 and Calyculin A

2003 ◽  
Vol 43 (5) ◽  
pp. 248-251
Author(s):  
Akiko KITA ◽  
Kunio MIKI
Keyword(s):  
Crystal Structure ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Calyculin A

scholarly journals Crystal structure of the complex between calyculin A and protein phosphatase 1 catalytic subunit

2002 ◽  
Vol 58 (s1) ◽  
pp. c103-c103
Author(s):  
A. Kita ◽  
S. Matsunaga ◽  
A. Takai ◽  
H. Kataiwa ◽  
T. Wakimoto ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Calyculin A

scholarly journals Crystal Structure of the Complex between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1

Structure ◽  
2002 ◽  
Vol 10 (5) ◽  
pp. 715-724 ◽  
Author(s):  
Akiko Kita ◽  
Shigeki Matsunaga ◽  
Akira Takai ◽  
Hirotaka Kataiwa ◽  
Toshiyuki Wakimoto ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Calyculin A

Crystal Structure of the Catalytic Subunit of Human Protein Phosphatase 1 and its Complex with Tungstate

1995 ◽  
Vol 254 (5) ◽  
pp. 942-959 ◽  
Author(s):  
Marie-Pierre Egloff ◽  
Patricia T.W. Cohen ◽  
Peter Reinemer ◽  
David Barford
Keyword(s):  
Crystal Structure ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Human Protein ◽  
Protein Phosphatase 1

scholarly journals Identification of Novel Serine/Threonine Protein Phosphatases inTrypanosoma cruzi: a Potential Role in Control of Cytokinesis and Morphology

2000 ◽  
Vol 68 (3) ◽  
pp. 1350-1358 ◽  
Author(s):  
George A. Orr ◽  
Craig Werner ◽  
Jun Xu ◽  
Marcia Bennett ◽  
Louis M. Weiss ◽  
...  
Keyword(s):  
Cell Division ◽  
Okadaic Acid ◽  
Blot Analysis ◽  
Protein Phosphatase ◽  
Protein Phosphatases ◽  
Growth Arrest ◽  
Human Protein ◽  
Protein Phosphatase 1 ◽  
Calyculin A ◽  
Metacyclic Trypomastigote

ABSTRACT We cloned two novel Trypanosoma cruzi proteins by using degenerate oligonucleotide primers prepared against conserved domains in mammalian serine/threonine protein phosphatases 1, 2A, and 2B. The isolated genes encoded proteins of 323 and 330 amino acids, respectively, that were more homologous to the catalytic subunit of human protein phosphatase 1 than to those of human protein phosphatase 2A or 2B. The proteins encoded by these genes have been tentatively designated TcPP1α and TcPP1β. Northern blot analysis revealed the presence of a major 2.3-kb mRNA transcript hybridizing to each gene in both the epimastigote and metacyclic trypomastigote developmental stages. Southern blot analysis suggests that each protein phosphatase 1 gene is present as a single copy in the T. cruzi genome. The complete coding region for TcPP1β was expressed inEscherichia coli by using a vector, pTACTAC, with thetrp-lac hybrid promoter. The recombinant protein from the TcPP1β construct displayed phosphatase activity toward phosphorylasea, and this activity was preferentially inhibited by calyculin A (50% inhibitory concentration [IC50], ∼2 nM) over okadaic acid (IC50, ∼100 nM). Calyculin A, but not okadaic acid, had profound effects on the in vitro replication and morphology of T. cruzi epimastigotes. Low concentrations of calyculin A (1 to 10 nM) caused growth arrest. Electron microscopic studies of the calyculin A-treated epimastigotes revealed that the organisms underwent duplication of organelles, including the flagellum, kinetoplast, and nucleus, but were incapable of completing cell division. At concentrations higher than 10 nM, or upon prolonged incubation at lower concentrations, the epimastigotes lost their characteristic elongated spindle shape and had a more rounded morphology. Okadaic acid at concentrations up to 1 μM did not result in growth arrest or morphological alterations to T. cruziepimastigotes. Calyculin A, but not okadaic acid, was also a potent inhibitor of the dephosphorylation of 32P-labeled phosphorylase a by T. cruzi epimastigotes and metacyclic trypomastigote extracts. These inhibitor studies suggest that in T. cruzi, type 1 protein phosphatases are important for the completion of cell division and for the maintenance of cell shape.

Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1

1993 ◽  
pp. 113-119
Author(s):  
Zhongjian Zhang ◽  
Sumin Zhao ◽  
Stephen Deans-Zirattu ◽  
Ge Bai ◽  
Ernest Y. C. Lee
Keyword(s):  
Protein Phosphatase ◽  
Muscle Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Rabbit Muscle

scholarly journals The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for regulation of the phosphorylation status of Fin1, a novel intermediate filament protein

2002 ◽  
Vol 365 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Isabel MAYORDOMO ◽  
Pascual SANZ
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcriptional Regulation ◽  
Intermediate Filament ◽  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Intermediate Filament Protein ◽  
Filament Protein ◽  
Two Hybrid ◽  
Hybrid Screening

In order to identify proteins that interact with Bmh2, a yeast member of the 14-3-3 protein family, we performed a two-hybrid screening using LexA-Bmh2 as bait. We identified Fin1, a novel intermediate filament protein, as the protein that showed the highest degree of interaction. We also identified components of the vesicular transport machinery such as Gic2 and Msb3, proteins involved in transcriptional regulation such as Mbf1, Gcr2 and Reg2, and a variety of other different proteins (Ppt1, Lre1, Rps0A and Ylr177w). We studied the interaction between Bmh2 and Fin1 in more detail and found that Bmh2 only interacted with phosphorylated forms of Fin1. In addition, we showed that Glc7, the catalytic subunit of the protein phosphatase 1 complex, was also able to interact with Fin1.

Mutational Analysis of the Catalytic Subunit of Muscle Protein Phosphatase-1†

Biochemistry ◽  
1996 ◽  
Vol 35 (20) ◽  
pp. 6276-6282 ◽  
Author(s):  
Jun Zhang ◽  
Zhongjian Zhang ◽  
Keith Brew ◽  
Ernest Y. C. Lee
Keyword(s):  
Protein Phosphatase ◽  
Mutational Analysis ◽  
Muscle Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1
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