A microbial sensor for discovering structural probes of protein misfolding and aggregation

บทความในวารสาร


ผู้เขียน/บรรณาธิการ


กลุ่มสาขาการวิจัยเชิงกลยุทธ์

ไม่พบข้อมูลที่เกี่ยวข้อง


รายละเอียดสำหรับงานพิมพ์

รายชื่อผู้แต่งWaraho-Zhmayev D., Gkogka L., Yu T.-Y., Delisa M.P.

ผู้เผยแพร่Taylor and Francis Group

ปีที่เผยแพร่ (ค.ศ.)2013

วารสารPrion (1933-6896)

Volume number7

Issue number2

หน้าแรก151

หน้าสุดท้าย156

จำนวนหน้า6

นอก1933-6896

eISSN1933-690X

URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84875459848&doi=10.4161%2fpri.23328&partnerID=40&md5=f6e400bd9a446a78c8620210fd5bd46a

ภาษาEnglish-Great Britain (EN-GB)


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บทคัดย่อ

In all cell types, protein homeostasis, or 'proteostasis,' is maintained by sophisticated quality control networks that regulate protein synthesis, folding, trafficking, aggregation, disaggregation, and degradation. In one notable example, Escherichia coli employ a proteostasis system that determines whether substrates of the twin-arginine translocation (Tat) pathway are correctly folded and thus suitable for transport across the tightly sealed cytoplasmic membrane. Herein, we review growing evidence that the Tat translocase itself discriminates folded proteins from those that are misfolded and/or aggregated, preferentially exporting only the former. Genetic suppressors that inactivate this mechanism have recently been isolated and provide direct evidence for the participation of the Tat translocase in structural proofreading of its protein substrates. We also discuss how this discriminatory 'folding sensor' has been exploited for the discovery of structural probes (e.g., sequence mutations, pharmacologic chaperones and intracellular antibodies) that modulate the folding and solubility of virtually any protein-of-interest, including those associated with aggregation diseases (e.g., a-synuclein and amyloid-฿ protein). Taken together, these studies highlight the utility of engineered bacteria for rapidly and inexpensively uncovering potent anti-aggregation factors. ฉ 2013 Landes Bioscience. ฉ 2013 Landes Bioscience.


คำสำคัญ

Amyloid-ß proteinAntibody therapiesChemical chaperonesDirected evolutionFolding quality controlHigh-throughput screeningProtein misfolding disordersProtein secretionα-synuclein


อัพเดทล่าสุด 2023-18-10 ถึง 07:42