Evidence map›Paper›PMID 29704042›Full record

ArticleApplied microbiology and biotechnology2018

Robust signal peptides for protein secretion in Yarrowia lipolytica: identification and characterization of novel secretory tags.

Ewelina Celińska, Monika Borkowska, Wojciech Białas, Paulina Korpys, Jean-Marc Nicaud

Abstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed.

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  17. Synthesis of Secretory Proteins inInternational journal of molecular sciences · 2022
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  19. Secretory helpers for enhanced production of heterologous proteins inBiotechnology reports (Amsterdam, Netherlands) · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Ewelina CelińskaDepartment of Biotechnology and Food Microbiology, Poznan University of Life Sciences, ul. Wojska Polskiego 48, 60-627, Poznań, Poland. ewelina.celinska@up.poznan.pl.ORCID http://orcid.org/0000-0001-8372-8459
Monika BorkowskaDepartment of Biotechnology and Food Microbiology, Poznan University of Life Sciences, ul. Wojska Polskiego 48, 60-627, Poznań, Poland.
Wojciech BiałasDepartment of Biotechnology and Food Microbiology, Poznan University of Life Sciences, ul. Wojska Polskiego 48, 60-627, Poznań, Poland.
Paulina KorpysDepartment of Biotechnology and Food Microbiology, Poznan University of Life Sciences, ul. Wojska Polskiego 48, 60-627, Poznań, Poland.
Jean-Marc NicaudINRA-AgroParisTech, UMR1319, Team BIMLip: Integrative Metabolism of Microbial Lipids, Domaine de Vilvert, Micalis Institute, 78352, Jouy-en-Josas, France.

Funding

European Molecular Biology Organization ASTF-117-2016Ministerstwo Nauki i Szkolnictwa Wyższego IP2015 011074
6 · The paper itself

Abstract

Upon expression of a given protein in an expression host, its secretion into the culture medium or cell-surface display is frequently advantageous in both research and industrial contexts. Hence, engineering strategies targeting folding, trafficking, and secretion of the proteins gain considerable interest. Yarrowia lipolytica has emerged as an efficient protein expression platform, repeatedly proved to be a competitive secretor of proteins. Although the key role of signal peptides (SPs) in secretory overexpression of proteins and their direct effect on the final protein titers are widely known, the number of reports on manipulation with SPs in Y. lipolytica is rather scattered. In this study, we assessed the potential of ten different SPs for secretion of two heterologous proteins in Y. lipolytica. Genomic and transcriptomic data mining allowed us to select five novel, previously undescribed SPs for recombinant protein secretion in Y. lipolytica. Their secretory potential was assessed in comparison with known, widely exploited SPs. We took advantage of Golden Gate approach, for construction of expression cassettes, and micro-volume enzymatic assays, for functional screening of large libraries of recombinant strains. Based on the adopted strategy, we identified novel secretory tags, characterized their secretory capacity, indicated the most potent SPs, and suggested a consensus sequence of a potentially robust synthetic SP to expand the molecular toolbox for engineering Y. lipolytica.

Indexed as

Fungal ProteinsIndustrial MicrobiologyProtein EngineeringProtein Sorting SignalsProtein TransportRecombinant ProteinsYarrowiaFungal ProteinsProtein Sorting SignalsRecombinant ProteinsLeader sequencesModular cloningProtein expressionProtein secretionSignal peptidesYarrowia lipolytica

Identifiers

PMID29704042
PMCPMC5959983

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.