NDLI: Novel protein–protein interactions of TPPII, p53, and SIRT7

Content Provider	Springer Nature Link
Author	Nahálková, Jarmila
Copyright Year	2015
Abstract	Novel protein–protein interactions of TPPII, SIRT7, and p53 were detected by co-immunoprecipitation using both HeLa cell lysates and the cytoplasmic fraction prepared by fractionation of mouse liver tissue. The interactions were further verified in vivo by in situ proximity ligation assay (PLA) within control HEK293 cells transformed with empty vector, $_{highact}$TPPII HEK293 cells over-expressing murine TPPII displaying high specific enzymatic activity and in $_{lowact}$TPPII HEK293 cells over-expressing human TPPII having low specific activity of the enzyme. Besides an abundant cytoplasmic localization of TPPII-p53 interaction signal, the nuclear interactions were also demonstrated. The cytoplasmic interactions were likewise detected between TPPII and SIRT7 in control HEK293 and $_{lowact}$TPPII HEK293 cells. The interactions of SIRT7 with p53 were confirmed in three HEK293 cell transformants as well. The cytoplasmic occurrence of SIRT7 protein was demonstrated by immunofluorescence, when both nucleolar and cytoplasmic signals were identified within HEK293 cells and primary human fibroblasts. The unique cytoplasmic localization of SIRT7 protein was discussed based on an epitope specificity of N-terminus specific SIRT7 antibodies utilized in the present study compared with C-terminus specific antibodies previously used for nuclear detection of SIRT7 by other authors. The epitope sequence of N-terminal antibodies is occurring in all three splicing variants of SIRT7 compared to the epitope of C-terminal antibody, which is specific exclusively to the splicing variant 1. The cytoplasmic localization of p53 detected by immunofluorescence supported the results from its interactions with TPPII and SIRT7 observed by in situ PLA within model cells. Novel interactions of TPPII, p53, and SIRT7 presented in this study might contribute to the knowledge of the regulatory effects of these proteins on apoptotic pathways and to the understanding mechanisms of aging and lifespan regulation.
Starting Page	13
Ending Page	22
Page Count	10
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	409
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Springer US
Publisher Date	2015-07-14
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	TPPII SIRT7 p53 Apoptosis Cellular senescence Aging Biochemistry Medical Biochemistry Oncology Cardiology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The protein-interaction network with functional roles in tumorigenesis, neurodegeneration, and aging

The BM2 protein of influenza B virus interacts with p53 and inhibits its transcriptional and apoptotic activities

Characterizing the novel protein p33MONOX

Tunicamycin suppresses cisplatin-induced HepG2 cell apoptosis via enhancing p53 protein nuclear export

Reactive oxygen species, mitochondria, apoptosis and aging

P53 and cell-cycle-regulated protein expression in small intestinal cells after fast-neutron irradiation in mice

Involvement of Annexin A2 in p53 induced apoptosis in lung cancer

Hyperglycemia induces apoptosis and p53 mobilization to mitochondria in RINm5F cells

Interactions of protein kinase CK2 subunits

Novel protein–protein interactions of TPPII, p53, and SIRT7

Similar Documents

The protein-interaction network with functional roles in tumorigenesis, neurodegeneration, and aging

The BM2 protein of influenza B virus interacts with p53 and inhibits its transcriptional and apoptotic activities

Characterizing the novel protein p33MONOX

Tunicamycin suppresses cisplatin-induced HepG2 cell apoptosis via enhancing p53 protein nuclear export

Reactive oxygen species, mitochondria, apoptosis and aging

P53 and cell-cycle-regulated protein expression in small intestinal cells after fast-neutron irradiation in mice

Involvement of Annexin A2 in p53 induced apoptosis in lung cancer

Hyperglycemia induces apoptosis and p53 mobilization to mitochondria in RINm5F cells

Interactions of protein kinase CK2 subunits

Novel protein–protein interactions of TPPII, p53, and SIRT7