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Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery

Bost, S.
Silva, Filo
Rudaz, C.
Published in Molecular Microbiology. 2000, vol. 38, no. 3, p. 575-587
Abstract A chimeric protein containing the uncleaved signal sequence of plasminogen activators inhibitor-2 (PAI2) fused to alkaline phosphatase (AP) interferes with Escherichia coli protein export and arrests growth. Suppressors of this toxicity include secG mutations that define the Thr-41-Leu-42-Phe-43 (TLF) domain of SecG. These mutations slow down the export of PAI2-AP. Another construct encoding a truncated PAI2 signal sequence (hB-AP) is also toxic. Most suppressors exert their effect on both chimeric proteins. We describe here five secG suppressors that only suppress the toxicity of hB-AP and selectively slow down its export. These mutations do not alter the TLF domain: three encode truncated SecG, whereas two introduce Arg residues in the transmembrane domains of SecG. The shortest truncated protein only contains 13 residues of SecG, suggesting that the mutation is equivalent to a null allele. Indeed, a secG disruption selectively suppresses the toxicity of hB-AP. However, the missense mutations are not null alleles. They allow SecG binding to SecYE, although with reduced affinity. Furthermore, these mutated SecG are functional, as they facilitate the export of endogenous proteins. Thus, SecG participates in signal sequence recognition, and both transmembrane domains of SecG contribute to ensure normal signal sequence recognition by the translocase.
Keywords Alkaline Phosphatase/chemistry/genetics/metabolismAllelesAmino Acid SequenceAmino Acid SubstitutionBacterial Proteins/ chemistry/ genetics/metabolismEscherichia coli/genetics/growth & development/ metabolismEscherichia coli ProteinsMembrane Proteins/ chemistry/ genetics/metabolismMolecular Sequence DataMutationPhenotypePlasminogen Activator Inhibitor 2/chemistry/genetics/metabolismPoint MutationPrecipitin TestsProtein Sorting SignalsProtein Structure, TertiaryProtein TransportRecombinant Fusion Proteins/chemistry/metabolismSequence Analysis, DNA
PMID: 11069681
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BOST, S. et al. Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery. In: Molecular Microbiology, 2000, vol. 38, n° 3, p. 575-587.

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Deposited on : 2010-08-27

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