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High-throughput Selection of Human de novo-emerged sORFs with High Folding Potential

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F24%3A00585603" target="_blank" >RIV/61388963:_____/24:00585603 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/24:10483116

  • Result on the web

    <a href="https://doi.org/10.1093/gbe/evae069" target="_blank" >https://doi.org/10.1093/gbe/evae069</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/gbe/evae069" target="_blank" >10.1093/gbe/evae069</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    High-throughput Selection of Human de novo-emerged sORFs with High Folding Potential

  • Original language description

    De novo genes emerge from previously noncoding stretches of the genome. Their encoded de novo proteins are generally expected to be similar to random sequences and, accordingly, with no stable tertiary fold and high predicted disorder. However, structural properties of de novo proteins and whether they differ during the stages of emergence and fixation have not been studied in depth and rely heavily on predictions. Here we generated a library of short human putative de novo proteins of varying lengths and ages and sorted the candidates according to their structural compactness and disorder propensity. Using Forster resonance energy transfer combined with Fluorescence-activated cell sorting, we were able to screen the library for most compact protein structures, as well as most elongated and flexible structures. We find that compact de novo proteins are on average slightly shorter and contain lower predicted disorder than less compact ones. The predicted structures for most and least compact de novo proteins correspond to expectations in that they contain more secondary structure content or higher disorder content, respectively. Our experiments indicate that older de novo proteins have higher compactness and structural propensity compared with young ones. We discuss possible evolutionary scenarios and their implications underlying the age-dependencies of compactness and structural content of putative de novo proteins.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GB14-36098G" target="_blank" >GB14-36098G: Center for tropical biology</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Genome Biology and Evolution

  • ISSN

    1759-6653

  • e-ISSN

    1759-6653

  • Volume of the periodical

    16

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    17

  • Pages from-to

    evae069

  • UT code for WoS article

    001204479300001

  • EID of the result in the Scopus database

    2-s2.0-85191082529