Dataset Information

The proteolytically inactive orthocaspase of Synechocystis sp. PCC 6803 plays an important role during oxidative stress

ABSTRACT: Caspases are proteases, best known for their involvement in the execution of apoptosis – a subtype of programmed cell death, which occurs only in animals. These proteases are composed of two structural building blocks: a proteolytically active p20 domain and a regulatory p10 domain. Although structural homologues appear in representatives of all other organisms, their functional homology, i. e. cell death depending on their proteolytical activity, is still much disputed. Additionally, pseudo-caspases and pseudo-metacaspases, in which the catalytic histidine-cysteine diad is substituted with non-proteolytic amino acid residues, were shown to be involved in cell death programmes. Here, we present the involvement of a pseudo-orthocaspase (SyOC), a prokaryotic caspase-homologue lacking the p10 domain, in oxidative stress in the model cyanobacterium Synechocystis sp. PCC 6803. To study the in vivo impact of this pseudo-protease during oxidative stress its gene expression during exposure to H2O2 was monitored by RT-qPCR. Furthermore, a knock-out mutant lacking the pseudo-orthocaspase gene was designed and its survival and growth rates were compared to wild type cells as well as its proteome. Deletion of SyOC led to cells with higher tolerance towards oxidative stress, the protein therefore might be involved in a pro-death pathway.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Synechocystis Sp. Pcc 6803

SUBMITTER: Franziska Voellmy

LAB HEAD: Christiane Funk

PROVIDER: PXD022955 | Pride | 2021-09-09

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20200727_OR16_UM7_Vollm004_EPICXS_SLema_Strap_sample10_1ug.raw	Raw
	20200727_OR16_UM7_Vollm004_EPICXS_SLema_Strap_sample11_1ug.raw	Raw
	20200727_OR16_UM7_Vollm004_EPICXS_SLema_Strap_sample12_1ug.raw	Raw
	20200727_OR16_UM7_Vollm004_EPICXS_SLema_Strap_sample13_1ug.raw	Raw
	20200727_OR16_UM7_Vollm004_EPICXS_SLema_Strap_sample14_1ug.raw	Raw

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Publications

The Role of Pseudo-Orthocaspase (SyOC) of <i>Synechocystis</i> sp. PCC 6803 in Attenuating the Effect of Oxidative Stress.

Lema A Saul S Klemenčič Marina M Völlmy Franziska F Altelaar Maarten M Funk Christiane C

Frontiers in microbiology 20210204

Caspases are proteases, best known for their involvement in the execution of apoptosis-a subtype of programmed cell death, which occurs only in animals. These proteases are composed of two structural building blocks: a proteolytically active p20 domain and a regulatory p10 domain. Although structural homologs appear in representatives of all other organisms, their functional homology, i.e., cell death depending on their proteolytical activity, is still much disputed. Additionally, pseudo-caspase ...[more]

PMID: 33613507

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Project description:This model is from the article: Systems biology analysis of programmed cell death Shani Bialik, Einat Zalckvar, Yaara Ber, Assaf D. Rubinstein, Adi Kimchi Trends in Biochemical Sciences Volume 35, Issue 10, 556-564, 27 May 2010 20537543 , Abstract: Systems biology, a combined computational and experimental approach to analyzing complex biological systems, has recently been applied to understanding the pathways that regulate programmed cell death. This approach has become especially crucial because recent advances have resulted in an expanded view of the network, to include not just a single death module (apoptosis) but multiple death programs, including programmed necrosis and autophagic cell death. Current research directions in the systems biology field range from quantitative analysis of subprocesses of individual death pathways to the study of interconnectivity among the various death modules of the larger network. These initial studies have provided great advances in our understanding of programmed cell death and have important clinical implications for drug target research. Brief Note about the model: This model is an export of 26 SPIKE Apoptosis Networks to SBML format. This is a pathway model (not quantitative model) of Apoptosis. Apoptosis, or type I cell death, is a form of programmed cell death characterized by fragmentation of the cytoplasm and nucleus, chromatin condensation and fragmentation, cytoskeletal collapse, membrane blebbing, and finally, disintegration of the cell into apoptotic bodies, which are engulfed by adjacent cells, thereby avoiding an inflammatory response. It serves to model tissues during embryonic development, to regulate cell number by eliminating excess cells, and to remove damaged, mutated or infected cells. Defective or excessive apoptosis can lead to cancer or autoimmune and degenerative diseases, respectively. Apoptosis is executed by a family of cysteine proteases, the caspases, which function in a proteolytic cascade that is initiated by either the intrinsic mitochondrial-based pathway leading to apoptosome formation, or the extrinsic pathway, which involves activation of death receptors by their extracellular ligands to form the DISC. The most distal caspases, known as the executioner caspases, cleave numerous cellular substrates, thereby leading to specific dismantling of the cell. Apoptosis is regulated by multiple proteins at several levels, including the Bcl-2 family, which regulate the release of apoptogenic factors from the mitochondria, and the IAP family, which regulate caspase activity, and is countered by survival signals eminating from the NF-kB signaling pathway. Although most of the regulation occurs at the post-translational level, involving protein-protein interactions, proteolysis, changes in subcellular localization and phosphorylation, transcriptional control, such as by p53, can also modulate the expression levels of several key apoptotic proteins. This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not. . To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.