alexa A Dynamic View of Protein Phosphatase 1 Interaction with its Inhibitors
ISSN: 2155-9821

Journal of Bioprocessing & Biotechniques
Open Access

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Research Article

A Dynamic View of Protein Phosphatase 1 Interaction with its Inhibitors

Sudhish Mishra1, Mandal A2, Gupta RC1 and Mandal PK2*
1Translational Science and Molecular Medicine, Michigan State University, Grand Rapids, MI 48202, USA
2Edward Waters College, Biology Program, Jacksonville, FL 32209, USA
Corresponding Author : Prabir K Mandal
Professor, Biology Program, Edward Waters College, USA
Tel: 904-470-8091
E-mail: [email protected]
Received April 13, 2015; Accepted April 24, 2015; Published April 29, 2015
Citation: Mishra S, Mandal A, Gupta RC, Mandal PK (2015) A Dynamic View of Protein Phosphatase 1 Interaction with its Inhibitors. J Bioprocess Biotech 5:221 doi: 10.4172/2155-9821.1000221
Copyright: © 2015 Mishra S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 

Abstract

Protein phosphatase 1 (PP1) is well known for their role in signal transduction and protein function. Together with its inhibitors 1 and 2, it regulates wide variety of cellular activities. We have amplified catalytic subunit of PP1 (PP1c) and its inhibitors 1 (I-1) and 2 (I-2) from dog cardiac mRNA by rt-PCR and cloned into bacterial expression vector pCRT7. Cloned genes were expressed in E. coli BL21 (DE3) pLysS by IPTG induction. Functional positive clones were identified by western blotting of bacterial lysate and polymerase chain reaction. Double transformed bacterial cells were also generated by transforming PP1c clone with either I-1 or I-2. Activity of PP1 was analyzed in whole bacterial lysate by measuring dephosphorylation of phos b. Activities of inhibitors were analyzed by their capability to inhibit PP1 from dephosphorylation of phos b. Our findings indicate differential regulation of PP1 by I-1 and I-2. Both expressed recombinant inhibitors 1 and 2 have high potency for inhibition of PP1 activity. Interestingly, I-2 co-expression caused increase in PP1c expression but no change in expression was observed when co-expressed with I-1.

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