Abstract
The protein translocations across mitochondrial membranes are carried out by specialized complexes, the Translocase of Outer Membrane (TOM) and Translocase of Inner Membrane (TIM). TIM23 translocon is responsible for translocating the mitochondrial matrix proteins across the mitochondrial inner membrane. Tim44 is an essential, peripheral membrane protein in TIM23 complex. Tim44 is tightly associated with the inner mitochondrial membrane on the matrix side. The Tim44 C-Terminal Domain (CTD) functions as an Inner Mitochondrial Membrane (IMM) anchor that recruits the Presequence protein Associated Motor (PAM) to the TIM23 channel. Using X-ray crystallographic and biochemical data, we show that the N-terminal helices A1 and A2 of Tim44 – CTD are crucial for its membrane tethering function. Based on our data, we propose a model showing how the N-terminal A1 and A2 amphipathic helices can either expose their hydrophobic face during membrane binding or conceal it in the soluble form. Therefore, the A1 and A2 helices of Tim44 may function as a membrane sensor.
Keywords: Mitochondria, peripheral membrane protein, translocation, TIM23, Tim44Mitochondria, peripheral membrane protein, translocation, TIM23, Tim44
Protein & Peptide Letters
Title: Membrane Binding Mechanism of Yeast Mitochondrial Peripheral Membrane Protzein TIM44
Volume: 18 Issue: 7
Author(s): Wenjun Cui, Ratnakar Josyula, Jingzhi Li, Zhengqing Fu and Bingdong Sha
Affiliation:
Keywords: Mitochondria, peripheral membrane protein, translocation, TIM23, Tim44Mitochondria, peripheral membrane protein, translocation, TIM23, Tim44
Abstract: The protein translocations across mitochondrial membranes are carried out by specialized complexes, the Translocase of Outer Membrane (TOM) and Translocase of Inner Membrane (TIM). TIM23 translocon is responsible for translocating the mitochondrial matrix proteins across the mitochondrial inner membrane. Tim44 is an essential, peripheral membrane protein in TIM23 complex. Tim44 is tightly associated with the inner mitochondrial membrane on the matrix side. The Tim44 C-Terminal Domain (CTD) functions as an Inner Mitochondrial Membrane (IMM) anchor that recruits the Presequence protein Associated Motor (PAM) to the TIM23 channel. Using X-ray crystallographic and biochemical data, we show that the N-terminal helices A1 and A2 of Tim44 – CTD are crucial for its membrane tethering function. Based on our data, we propose a model showing how the N-terminal A1 and A2 amphipathic helices can either expose their hydrophobic face during membrane binding or conceal it in the soluble form. Therefore, the A1 and A2 helices of Tim44 may function as a membrane sensor.
Export Options
About this article
Cite this article as:
Cui Wenjun, Josyula Ratnakar, Li Jingzhi, Fu Zhengqing and Sha Bingdong, Membrane Binding Mechanism of Yeast Mitochondrial Peripheral Membrane Protzein TIM44, Protein & Peptide Letters 2011; 18 (7) . https://dx.doi.org/10.2174/092986611795445996
DOI https://dx.doi.org/10.2174/092986611795445996 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
![](/images/wayfinder.jpg)
- Author Guidelines
- Bentham Author Support Services (BASS)
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Pulmonary Infections in the Era of Biological Agents
Current Respiratory Medicine Reviews HIV Compartmentalization: A Review on a Clinically Important Phenomenon
Current HIV Research Live Recombinant Vectors for AIDS Vaccine Development
Current Molecular Medicine Thalidomide as an Immunotherapeutic Agent: The Effects on Neutrophil- Mediated Inflammation
Current Pharmaceutical Design Computer-aided Drug Design Investigations for Benzothiazinone Derivatives Against Tuberculosis
Combinatorial Chemistry & High Throughput Screening Exosomes: Critical Mediators of Tumour Microenvironment Reprogramming
Current Medicinal Chemistry Challenges and Opportunities of Nanotechnological based Approach for the Treatment of Tuberculosis
Current Pharmaceutical Design Regulation of Adaptive Immunity by the Neurotransmitter Norepinephrine
Current Immunology Reviews (Discontinued) Artificial Neural Network Methods Applied to Drug Discovery for Neglected Diseases
Combinatorial Chemistry & High Throughput Screening Understanding Recognition and Self-assembly in Biology using the Chemist´s Toolbox. Insight into Medicinal Chemistry
Current Topics in Medicinal Chemistry A Method to Prepare Solid Lipid Nanoparticles with Improved Entrapment Efficiency of Hydrophilic Drugs
Current Nanoscience Stereochemistry at the Forefront in the Design and Discovery of Novel Anti-tuberculosis Agents
Current Topics in Medicinal Chemistry Potential Therapeutic Agents from the Red Sea Organisms
Medicinal Chemistry Fusing Docking Scoring Functions Improves the Virtual Screening Performance for Discovering Parkinson's Disease Dual Target Ligands
Current Neuropharmacology Molecular Interactions in Interleukin and Toll-like Receptor Signaling Pathways
Current Pharmaceutical Design Induction of Cytochromes P450
Current Drug Metabolism Adrenocortical Crisis Triggered by Levothyroxine in an Unrecognized Autoimmune Polyglandular Syndrome Type-2: A Case Report with Review of the Literature
Current Drug Safety Natural Compounds Therapeutic Features in Brain Disorders by Experimental, Bioinformatics and Cheminformatics Methods
Current Medicinal Chemistry Targeting Breast Cancer Cells with G4 PAMAM Dendrimers and Valproic Acid Derivative Complexes
Anti-Cancer Agents in Medicinal Chemistry Synthesis, p38 Kinase Inhibitory and Anti-inflammatory Activity of New Substituted Benzimidazole Derivatives
Medicinal Chemistry