4.6 Article

Prediction of partial membrane protein topologies using a consensus approach

期刊

PROTEIN SCIENCE
卷 11, 期 12, 页码 2974-2980

出版社

WILEY
DOI: 10.1110/ps.0226702

关键词

membrane protein; topology; consensus prediction

向作者/读者索取更多资源

We have developed a method to reliably identify partial membrane protein topologies using the consensus of five topology prediction methods. When evaluated on a test set of experimentally characterized proteins, we find that approximately 90% of the partial consensus topologies are correctly predicted in membrane proteins from prokaryotic as well as eukaryotic organisms. Whole-genome analysis reveals that a reliable partial consensus topology can be predicted for similar to70% of all membrane proteins in a typical bacterial genome and for similar to55% of all membrane proteins in a typical eukaryotic genome. The average fraction of sequence length covered by a partial consensus topology is 44% for the prokaryotic proteins and 17% for the eukaryotic proteins in our test set, and similar numbers are found when the algorithm is applied to whole genomes. Reliably predicted partial topologies may simplify experimental determinations of membrane protein topology.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

Article Multidisciplinary Sciences

Effects of protein size, thermodynamic stability, and net charge on cotranslational folding on the ribosome

Jose Arcadio Farias-Rico, Frida Ruud Selin, Ioanna Myronidi, Marie Fruehauf, Gunnar von Heijne

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2018)

Article Biochemistry & Molecular Biology

Cotranslational Folding of a Pentarepeat β-Helix Protein

Luigi Notari, Markel Martinez-Carranza, Jose Arcadio Farias-Rico, Pal Stenmark, Gunnar von Heijne

JOURNAL OF MOLECULAR BIOLOGY (2018)

Article Biochemistry & Molecular Biology

Murine astrotactins 1 and 2 have a similar membrane topology and mature via endoproteolytic cleavage catalyzed by a signal peptidase

Patricia Lara, Asa Tellgren-Roth, Hourinaz Behesti, Zachi Horn, Nina Schiller, Karl Enquist, Malin Cammenberg, Amanda Liljenstrom, Mary E. Hatten, Gunnar von Heijne, IngMarie Nilsson

JOURNAL OF BIOLOGICAL CHEMISTRY (2019)

Article Biology

Structural and mutational analysis of the ribosome-arresting human XBP1u

Vivekanandan Shanmuganathan, Nina Schiller, Anastasia Magoulopoulou, Jingdong Cheng, Katharina Braunger, Florian Cymer, Otto Berninghausen, Birgitta Beatrix, Kenji Kohno, Gunnar von Heijne, Roland Beckmann

Article Biochemistry & Molecular Biology

Dynamic membrane topology in an unassembled membrane protein

Maximilian Seurig, Moira Ek, Gunnar von Heijne, Nir Fluman

NATURE CHEMICAL BIOLOGY (2019)

Article Cardiac & Cardiovascular Systems

Metabolomic Profile in HFpEF vs HFrEF Patients

Camilla Hage, Lars Lofgren, Filippos Michopoulos, Ralph Nilsson, Pia Davidsson, Chanchal Kumar, Mattias Ekstrom, Maria J. Eriksson, Patrik Lynga, Bengt Persson, Hakan Wallen, Li Ming Gan, Hans Persson, Cecilia Linde

JOURNAL OF CARDIAC FAILURE (2020)

Article Multidisciplinary Sciences

Cotranslational folding cooperativity of contiguous domains of α-spectrin

Grant Kemp, Ola B. Nilsson, Pengfei Tian, Robert B. Best, Gunnar von Heijne

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2020)

Article Biochemistry & Molecular Biology

Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli

Rageia Elfageih, Alexandros Karyolaimos, Grant Kemp, Jan-Willem de Gier, Gunnar von Heijne, Renuka Kudva

PROTEIN SCIENCE (2020)

Article Biology

Residue-by-residue analysis of cotranslational membrane protein integration in vivo

Felix Nicolaus, Ane Metola, Daphne Mermans, Amanda Liljenstrom, Ajda Krc, Salmo Mohammed Abdullahi, Matthew Zimmer, Thomas F. Miller, Gunnar von Heijne

Summary: The study investigates the cotranslational biosynthesis of E. coli inner membrane proteins and reveals the complexities in membrane integration process, including protein folding in the ribosome exit tunnel and interactions between charged residues and the membrane. The results also suggest residue-specific interactions between transmembrane helices during the integration process, supporting the 'sliding' model of translocon-mediated membrane protein integration.
Editorial Material Multidisciplinary Sciences

Molten globules lure transmembrane helices away from the membrane

Gunnar von Heijne

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2021)

Article Biochemistry & Molecular Biology

Upstream charged and hydrophobic residues impact the timing of membrane insertion of transmembrane helices

Felix Nicolaus, Fatima Ibrahimi, Anne den Besten, Gunnar von Heijne

Summary: During the cotranslational insertion of membrane proteins mediated by SecYEG, both electrostatic and hydrophobic interactions involving sequence elements can impact the behavior of transmembrane helices, leading to delayed contact with the membrane.

FEBS LETTERS (2022)

Article Biotechnology & Applied Microbiology

SignalP 6.0 predicts all five types of signal peptides using protein language models

Felix Teufel, Jose Juan Almagro Armenteros, Alexander Rosenberg Johansen, Magnus Halldor Gislason, Silas Irby Pihl, Konstantinos D. Tsirigos, Ole Winther, Soren Brunak, Gunnar von Heijne, Henrik Nielsen

Summary: Signal peptides are short amino acid sequences that regulate protein secretion and translocation. SignalP 6.0, a machine learning model, is introduced to detect all types of signal peptides, including those applicable to metagenomic data.

NATURE BIOTECHNOLOGY (2022)

Article Multidisciplinary Sciences

Cotranslational folding and assembly of the dimeric Escherichia coli inner membrane protein EmrE

Daphne Mermans, Felix Nicolaus, Klara Fleisch, Gunnar von Heijne

Summary: In recent years, it has been discovered that many cytoplasmic proteins can dimerize while being translated. However, it was unclear whether this phenomenon also applies to integral membrane proteins. This study demonstrates that the inner membrane protein EmrE in Escherichia coli can indeed undergo cotranslational interactions, suggesting that membrane proteins can start to fold and dimerize during the membrane insertion process.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2022)

Article Biochemistry & Molecular Biology

Cotranslational folding of human growth hormone in vitro and in Escherichia coli

Daphne Mermans, Felix Nicolaus, Aysel Baygin, Gunnar von Heijne

Summary: Human growth hormone (hGH) is a protein with four helix bundles and has pharmacological interest. This study investigates the folding of hGH during expression in Escherichia coli, both in vitro translation with or without the chaperone trigger factor (TF) and in E. coli. The findings suggest that hGH begins folding before it is fully released from the ribosome and may interact with TF and other chaperones.

FEBS LETTERS (2023)

Article Biology

Detecting sequence signals in targeting peptides using deep learning

Jose Juan Almagro Armenteros, Marco Salvatore, Olof Emanuelsson, Ole Winther, Gunnar von Heijne, Arne Elofsson, Henrik Nielsen

LIFE SCIENCE ALLIANCE (2019)

暂无数据