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The role of signal sequence proximal residues in the mature region of bacterial secreted proteins in E. coli.
Musik, Joanna E; Zalucki, Yaramah M; Beacham, Ifor R; Jennings, Michael P.
Afiliação
  • Musik JE; Institute for Glycomics, Griffith University, Gold Coast Campus, Gold Coast, QLD, 4222, Australia.
  • Zalucki YM; Institute for Glycomics, Griffith University, Gold Coast Campus, Gold Coast, QLD, 4222, Australia. Electronic address: y.zalucki@griffith.edu.au.
  • Beacham IR; Institute for Glycomics, Griffith University, Gold Coast Campus, Gold Coast, QLD, 4222, Australia.
  • Jennings MP; Institute for Glycomics, Griffith University, Gold Coast Campus, Gold Coast, QLD, 4222, Australia. Electronic address: m.jennings@griffith.edu.au.
Biochim Biophys Acta Biomembr ; 1864(10): 184000, 2022 10 01.
Article em En | MEDLINE | ID: mdl-35798072
ABSTRACT
Secreted proteins contain an N-terminal signal peptide to guide them through the secretion pathway. Once the protein is translocated, the signal peptide is removed by a signal peptidase, such as signal peptidase I. The signal peptide has been extensively studied and reviewed; however, the mature region has not been the focus of review. Here we cover the experimental evidence that highlights the important role of the mature region amino acid residues in both the efficiency and the ability of secreted proteins to be successfully exported via secretion pathways and cleaved by signal peptidase I.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Sinais Direcionadores de Proteínas / Escherichia coli Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Sinais Direcionadores de Proteínas / Escherichia coli Idioma: En Ano de publicação: 2022 Tipo de documento: Article