Evidence map›Paper›PMID 21424760›Full record

ArticleJournal of molecular evolution2011

Novel hydrophobins from Trichoderma define a new hydrophobin subclass: protein properties, evolution, regulation and processing.

Verena Seidl-Seiboth, Sabine Gruber, Ugur Sezerman, Torsten Schwecke, Aydin Albayrak, Torsten Neuhof, Hans von Döhren, Scott E Baker, Christian P Kubicek

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Article in Journal of molecular evolution, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

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0cells of the map it votes in
26citing papers in PubMed
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1 · What the graph read from it

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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.

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

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  8. Microorganisms · 2022
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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Verena Seidl-SeibothResearch Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorferstrasse 1a/166-5, 1060, Vienna, Austria.
Sabine Gruber
Ugur Sezerman
Torsten Schwecke
Aydin Albayrak
Torsten Neuhof
Hans von Döhren
Scott E Baker
Christian P Kubicek

Funding

Austrian Science Fund FWF T 390
6 · The paper itself

Abstract

Hydrophobins are small proteins, characterised by the presence of eight positionally conserved cysteine residues, and are present in all filamentous asco- and basidiomycetes. They are found on the outer surfaces of cell walls of hyphae and conidia, where they mediate interactions between the fungus and the environment. Hydrophobins are conventionally grouped into two classes (class I and II) according to their solubility in solvents, hydropathy profiles and spacing between the conserved cysteines. Here we describe a novel set of hydrophobins from Trichoderma spp. that deviate from this classification in their hydropathy, cysteine spacing and protein surface pattern. Phylogenetic analysis shows that they form separate clades within ascomycete class I hydrophobins. Using T. atroviride as a model, the novel hydrophobins were found to be expressed under conditions of glucose limitation and to be regulated by differential splicing.

Indexed as

Amino Acid SequenceAscomycotaCysteineEvolution, MolecularFungal ProteinsGlucoseHypocreaMolecular Sequence DataPhylogenyProtein SplicingSequence AlignmentSolubilitySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTrichodermaCysteineFungal ProteinsGlucose

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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.