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The positive inside rule is stronger when followed by a transmembrane helix

Minttu T. Virkki, Christoph Peters, Daniel Nilsson, Therese Sörensen, Susana Cristobal, Björn Wallner, View ORCID ProfileArne Elofsson
doi: https://doi.org/10.1101/014175
Minttu T. Virkki
aScience for Life Laboratory, Stockholm University SE-171 21 Solna, Sweden
bDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden
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Christoph Peters
aScience for Life Laboratory, Stockholm University SE-171 21 Solna, Sweden
bDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden
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Daniel Nilsson
bDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden
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Therese Sörensen
bDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden
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Susana Cristobal
dDepartment of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden
fDepartments of Physiology, IKERBASQUE, Basque Foundation for Science, Faculty of Medicine and Dentistry, University of the Basque Country, Leioa, Spain
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Björn Wallner
dDepartment of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden
fDepartments of Physiology, IKERBASQUE, Basque Foundation for Science, Faculty of Medicine and Dentistry, University of the Basque Country, Leioa, Spain
cSwedish e-Science Research Center (SeRC)
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Arne Elofsson
aScience for Life Laboratory, Stockholm University SE-171 21 Solna, Sweden
bDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden
cSwedish e-Science Research Center (SeRC)
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  • ORCID record for Arne Elofsson
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Abstract

The translocon recognizes transmembrane helices with sufficient level of hydrophobicity and inserts them into the membrane. However, sometimes less hydrophobic helices are also recognized. Positive inside rule, orientational preferences of and specific interactions with neighboring helices have been shown to aid in the recognition of these helices, at least in artificial systems. To better understand how the translocon inserts marginally hydrophobic helices, we studied three naturally occurring marginally hydrophobic helices, which were previously shown to require the subsequent helix for efficient translocon recognition. We find no evidence for specific interactions when we scan all residues in the subsequent helices. Instead, we identify arginines located at the N-terminal part of the subsequent helices that are crucial for the recognition of the marginally hydrophobic transmembrane helices, indicating that the positive inside rule is important. However, in two of the constructs these arginines do not aid in the recognition without the rest of the subsequent helix, i.e. the positive inside rule alone is not sufficient. Instead, the improved recognition of marginally hydrophobic helices can here be explained as follows; the positive inside rule provides an orientational preference of the subsequent helix, which in turn allows the marginally hydrophobic helix to be inserted, i.e. the effect of the positive inside rule is stronger if positively charged residues are followed by a transmembrane helix. Such a mechanism can obviously not aid C-terminal helices and consequently we find that the terminal helices in multi-spanning membrane proteins are more hydrophobic than internal helices.

Footnotes

  • Email addresses: minttu.virkki{at}scilifelab.se (Minttu T. Virkki), christoph.peters{at}scilifelab.se (Christoph Peters), daniel.nilsson{at}dbb.su.se (Daniel Nilsson), therese{at}cormentia.se (Therese Sörensen), susana.cristobal{at}liu.se (Susana Cristobal), bjorn.wallner{at}liu.se (Björn Wallner), arne{at}bioinfo.se (Arne Elofsson)

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
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Posted January 23, 2015.
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The positive inside rule is stronger when followed by a transmembrane helix
Minttu T. Virkki, Christoph Peters, Daniel Nilsson, Therese Sörensen, Susana Cristobal, Björn Wallner, Arne Elofsson
bioRxiv 014175; doi: https://doi.org/10.1101/014175
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The positive inside rule is stronger when followed by a transmembrane helix
Minttu T. Virkki, Christoph Peters, Daniel Nilsson, Therese Sörensen, Susana Cristobal, Björn Wallner, Arne Elofsson
bioRxiv 014175; doi: https://doi.org/10.1101/014175

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