The function of a leader peptide in translocating charged amino acyl residues across a membrane

Rohrer, Jack; Kuhn, Andreas

doi:10.1126/science.2124001

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	The function of a leader peptide in translocating charged amino acyl residues across a membrane
Authors:	Rohrer, Jack Kuhn, Andreas
DOI:	10.1126/science.2124001
Published in:	Science
Volume(Issue):	250
Issue:	4986
Page(s):	1418
Pages to:	1421
Issue Date:	7-Dec-1990
Publisher / Ed. Institution:	American Association for the Advancement of Science
ISSN:	0036-8075 1095-9203
Language:	English
Subject (DDC):	572: Biochemistry
Abstract:	Insertion of bacteriophage coat proteins into the membrane of infected bacterial cells can be studied as a model system of protein translocation across membranes. The coat protein of the filamentous bacteriophage Pf3 – which infects Pseudomonas aeruginosa – is 44 amino acids in length and has the same basic structure as the coat protein of bacteriophage M13, which infects Escherichia coli. However, unlike the Pf3 coat protein, the M13 coat protein is synthesized as a precursor (procoat) with a typical leader (signal) sequence, which is cleaved after membrane insertion. Nevertheless, when the gene encoding the Pf3 coat protein is expressed in E. coli, the protein is translocated across the membrane. Hybrid M13 and Pf3 coat proteins were constructed in an attempt to understand how the Pf3 coat protein is translocated without a leader sequence. These studies demonstrated that the extracellular regions of the proteins determined their cellular location. When three charged residues in this region were neutralized, the leader-free M13 coat protein was also inserted into the membrane. Differences in the water shell surrounding these residues may account for efficient membrane insertion of the protein without a leader sequence.
URI:	https://digitalcollection.zhaw.ch/handle/11475/6844
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Appears in collections:	Publikationen Life Sciences und Facility Management

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Rohrer, J., & Kuhn, A. (1990). The function of a leader peptide in translocating charged amino acyl residues across a membrane. Science, 250(4986), 1418–1421. https://doi.org/10.1126/science.2124001

Rohrer, J. and Kuhn, A. (1990) ‘The function of a leader peptide in translocating charged amino acyl residues across a membrane’, Science, 250(4986), pp. 1418–1421. Available at: https://doi.org/10.1126/science.2124001.

J. Rohrer and A. Kuhn, “The function of a leader peptide in translocating charged amino acyl residues across a membrane,” Science, vol. 250, no. 4986, pp. 1418–1421, Dec. 1990, doi: 10.1126/science.2124001.

ROHRER, Jack und Andreas KUHN, 1990. The function of a leader peptide in translocating charged amino acyl residues across a membrane. Science. 7 Dezember 1990. Bd. 250, Nr. 4986, S. 1418–1421. DOI 10.1126/science.2124001

Rohrer, Jack, and Andreas Kuhn. 1990. “The Function of a Leader Peptide in Translocating Charged Amino Acyl Residues across a Membrane.” Science 250 (4986): 1418–21. https://doi.org/10.1126/science.2124001.

Rohrer, Jack, and Andreas Kuhn. “The Function of a Leader Peptide in Translocating Charged Amino Acyl Residues across a Membrane.” Science, vol. 250, no. 4986, Dec. 1990, pp. 1418–21, https://doi.org/10.1126/science.2124001.