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dc.contributor.authorRohrer, Jack-
dc.contributor.authorKuhn, Andreas-
dc.date.accessioned2018-06-13T10:00:14Z-
dc.date.available2018-06-13T10:00:14Z-
dc.date.issued1990-12-07-
dc.identifier.issn0036-8075de_CH
dc.identifier.issn1095-9203de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/6844-
dc.description.abstractInsertion 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.de_CH
dc.language.isoende_CH
dc.publisherAmerican Association for the Advancement of Sciencede_CH
dc.relation.ispartofSciencede_CH
dc.rightsLicence according to publishing contractde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleThe function of a leader peptide in translocating charged amino acyl residues across a membranede_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
dc.identifier.doi10.1126/science.2124001de_CH
zhaw.funding.euNode_CH
zhaw.issue4986de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end1421de_CH
zhaw.pages.start1418de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume250de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
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.


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