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MGR2 Sale

目录号 : GC44190

A negative control for MGR1

MGR2 Chemical Structure

Cas No.:2361529-47-5

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5mg
¥599.00
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10mg
¥1,079.00
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25mg
¥2,399.00
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Sample solution is provided at 25 µL, 10mM.

产品文档

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产品描述

MGR2 is a negative control compound for the activity of the reactive oxygen species-generating probe MGR1. Unlike MGR1, MGR2 does not induce superoxide production or cell death in HEK293T cells.

Chemical Properties

Cas No. 2361529-47-5 SDF
Canonical SMILES O=C(C(C)(C)C)OCOC1=C(C=CC=C2)C2=CC=C1
分子式 C16H18O3 分子量 258.3
溶解度 DMF: 30 mg/ml,DMSO: 30 mg/ml,Ethanol: 30 mg/ml 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 3.8715 mL 19.3573 mL 38.7147 mL
5 mM 0.7743 mL 3.8715 mL 7.7429 mL
10 mM 0.3871 mL 1.9357 mL 3.8715 mL
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Research Update

MGR2 regulates mitochondrial preprotein import by associating with channel-forming Tim23 subunit

Mol Biol Cell 2020 May 15;31(11):1112-1123.PMID:32186971DOI:10.1091/mbc.E19-12-0677.

MGR2, a newly identified subunit of the TIM23 complex, functions as a gatekeeper of presequence translocase and thereby maintains quality control of inner membrane preproteins sorting. However, precise recruitment of the MGR2 subunit to the core channel and how it influences the assembly of the TIM23 complex during lateral sorting of preproteins are poorly understood. Present findings provide insights into a direct association of MGR2 with the channel-forming Tim23 subunit. Furthermore, the mutational analysis uncovers the TM1 region of MGR2 critically required for association with Tim23 and Tim21. On the other hand, the TM2 region of MGR2 is involved in bridging respiratory complexes to the TIM23 complex via Tim21. Importantly, both TM regions of MGR2 are essential for lateral sorting of preprotein into the inner membrane, as well as maintaining mitochondrial morphology. Together, our findings provide mechanistic insights into the role of MGR2 in regulating the dynamicity of the TIM23 complex assembly required for preprotein import and coupling of respiratory pathways.

The MGR2 subunit of the TIM23 complex regulates membrane insertion of marginal stop-transfer signals in the mitochondrial inner membrane

FEBS Lett 2020 Mar;594(6):1081-1087.PMID:31764998DOI:10.1002/1873-3468.13692.

The TIM23 complex mediates membrane insertion of presequence-containing mitochondrial proteins via a stop-transfer mechanism. Stop-transfer signals consist of hydrophobic transmembrane segments and flanking charges. MGR2 functions as a lateral gatekeeper of the TIM23 complex. However, it remains elusive which features of stop-transfer signals are discriminated by MGR2. To determine the effects of MGR2 on the TIM23-mediated stop-transfer pathway, we measured membrane insertion of model transmembrane segments of varied hydrophobicity and flanking charges in Mgr2-deletion or -overexpression yeast strains. We found that upon deletion of MGR2, the threshold hydrophobicity for membrane insertion, as well as the requirement for matrix-facing positive charges, is reduced. These results imply that the Mgr2-mediated gatekeeper function is important for controlling membrane sorting of marginal stop-transfer signals.

MGR2 functions as lateral gatekeeper for preprotein sorting in the mitochondrial inner membrane

Mol Cell 2014 Dec 4;56(5):641-52.PMID:25454944DOI:10.1016/j.molcel.2014.10.010.

The majority of preproteins destined for mitochondria carry N-terminal presequences. The presequence translocase of the inner mitochondrial membrane (TIM23 complex) plays a central role in protein sorting. Preproteins are either translocated through the TIM23 complex into the matrix or are laterally released into the inner membrane. We report that the small hydrophobic protein MGR2 controls the lateral release of preproteins. MGR2 interacts with preproteins in transit through the TIM23 complex. Overexpression of MGR2 delays preprotein release, whereas a lack of MGR2 promotes preprotein sorting into the inner membrane. Preproteins with a defective inner membrane sorting signal are translocated into the matrix in wild-type mitochondria but are released into the inner membrane in Mgr2-deficient mitochondria. We conclude that MGR2 functions as a lateral gatekeeper of the mitochondrial presequence translocase, providing quality control for the membrane sorting of preproteins.

MGR2 promotes coupling of the mitochondrial presequence translocase to partner complexes

J Cell Biol 2012 May 28;197(5):595-604.PMID:22613836DOI:10.1083/jcb.201110047.

Many mitochondrial proteins are synthesized with N-terminal presequences in the cytosol. The presequence translocase of the inner mitochondrial membrane (TIM23) translocates preproteins into and across the membrane and associates with the matrix-localized import motor. The TIM23 complex consists of three core components and Tim21, which interacts with the translocase of the outer membrane (TOM) and the respiratory chain. We have identified a new subunit of the TIM23 complex, the inner membrane protein MGR2. Mitochondria lacking MGR2 were deficient in the Tim21-containing sorting form of the TIM23 complex. MGR2 was required for binding of Tim21 to TIM23(CORE), revealing a binding chain of TIM23(CORE)-Mgr2/Tim21-respiratory chain. Mgr2-deficient yeast cells were defective in growth at elevated temperature, and the mitochondria were impaired in TOM-TIM23 coupling and the import of presequence-carrying preproteins. We conclude that MGR2 is a coupling factor of the presequence translocase crucial for cell growth at elevated temperature and for efficient protein import.

The great escape: MGR2 of the mitochondrial TIM23 translocon is a gatekeeper Tasked with releasing membrane proteins

Mol Cell 2014 Dec 4;56(5):613-4.PMID:25479635DOI:10.1016/j.molcel.2014.11.022.

By using a combination of biochemistry and genetics, in this issue of Molecular CellIeva et al. (2014) uncover an unexpected role for MGR2 of the mitochondrial TIM23 translocon as a gatekeeper in the release of membrane proteins from the translocon.