TAILIEUCHUNG - Báo cáo khoa học: Signal peptide hydrophobicity is critical for early stages in protein export by Bacillus subtilis

Signal peptides that direct protein export inBacillus subtilisare overall more hydrophobic than signal peptides inEscherichia coli. To study the importance of signal peptide hydrophobicity for protein export in both organisms, the a-amylase AmyQ was provided with leucine-rich (high hydrophobicity) or alanine-rich (low hydrophobicity) signal peptides. AmyQ export was most efficiently directed by the authentic signal peptide, both in E. coliand B. subtilis. | ềFEBS Journal Signal peptide hydrophobicity is critical for early stages in protein export by Bacillus subtilis Geeske Zanen1 Edith N. G. Houben2 Rob Meima2 Harold Tjalsma3 t Jan D. H. Jongbloed3 i Helga Westers1 3 Bauke Oudega2 Joen Luirink2 Jan Maarten van Dijl1 and Wim J. Quax1 1 Department of PharmaceuticalBiology University of Groningen the Netherlands 2 Department of Molecular Microbiology Vrije Universiteit Amsterdam the Netherlands 3 Department of Genetics Groningen Biomolecular Sciences and Biotechnology Institute University of Groningen the Netherlands Keywords SRP signalpeptide protein targeting protein translocation trigger factor Correspondence W. J. Quax Department of Pharmaceutical Biology University of Groningen Antonius Deusinglaan 1 9713 AV Groningen the Netherlands Fax 31 50 3633000 Tel 31 50 3632558 E-mail Present addresses DSM Food Specialties Postbus 1 2600 MA Delft the Netherlands TDepartment of ClinicalChemistry University Medical Centre Nijmegen PO Box 9101 6500 HB Nijmegen the Netherlands Department of ClinicalGenetics University MedicalCenter of Groningen box 30001 9700 RB Groningen the Netherlands Laboratory of Molecular Bacteriology Department of MedicalMicrobiology University Medical Center of Groningen and University of Groningen Hanzeplein 1 PO Box 30001 9700 RB Groningen the Netherlands Received 29 March 2005 revised 03 May 2005 accepted 18 May 2005 doi Signal peptides that direct protein export in Bacillus subtilis are overall more hydrophobic than signal peptides in Escherichia coli. To study the importance of signal peptide hydrophobicity for protein export in both organisms the a-amylase AmyQ was provided with leucine-rich high hydrophobicity or alanine-rich low hydrophobicity signal peptides. AmyQ export was most efficiently directed by the authentic signal peptide both in E. coli and B. subtilis. The leucine-rich signal peptide directed AmyQ export less efficiently in .

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