Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway

Author:

Choi Hyun-Kyu123ORCID,Min Duyoung45ORCID,Kang Hyunook2ORCID,Shon Min Ju23ORCID,Rah Sang-Hyun123ORCID,Kim Hak Chan2ORCID,Jeong Hawoong1ORCID,Choi Hee-Jung2ORCID,Bowie James U.4ORCID,Yoon Tae-Young23ORCID

Affiliation:

1. Department of Physics, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.

2. School of Biological Sciences, Seoul National University, Seoul 08826, South Korea.

3. Institute for Molecular Biology and Genetics, Seoul National University, Seoul 08826, South Korea.

4. Department of Chemistry and Biochemistry, University of California–Los Angeles, Los Angeles, CA 90095, USA.

5. Department of Chemistry, Ulsan National Institute of Science and Technology, Ulsan 44919, South Korea.

Abstract

A pathway for helical membrane proteins Membrane proteins are inserted into cell membranes while they are being translated and may fold concurrently into their secondary and tertiary structures. Choi et al. describe a single-molecule force microscopy technique that allowed them to monitor folding of helical membrane proteins in vesicles and bicelles. Two helical membrane proteins, the Escherichia coli rhomboid protease GlpG and the human β 2 -adrenergic receptor, both folded from the N to the C terminus, with structures forming in units of helical hairpins. In the cell, this would allow these proteins to begin folding while being translated. Science , this issue p. 1150

Funder

National Institutes of Health

National Research Foundation of Korea

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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