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Nature

Resumen/Descripción – provisto por la editorial en inglés

Nature is a weekly international journal publishing the finest peer-reviewed research in all fields of science and technology on the basis of its originality, importance, interdisciplinary interest, timeliness, accessibility, elegance and surprising conclusions. Nature also provides rapid, authoritative, insightful and arresting news and interpretation of topical and coming trends affecting science, scientists and the wider public.

Palabras clave – provistas por la editorial

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Información

Tipo de recurso:

revistas

ISSN impreso

0028-0836

ISSN electrónico

1476-4687

Editor responsable

Springer Nature

País de edición

Reino Unido

Fecha de publicación

1869-

Cobertura temática

Ciencias naturales

Ingeniería y tecnología

Ciencias médicas y de la salud

Ciencias agrícolas y veterinarias

Tabla de contenidos

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doi: 10.1038/s41586-022-04779-x

Differential cofactor dependencies define distinct types of human enhancers

Christoph Neumayr; Vanja Haberle; Leonid Serebreni; Katharina Karner; Oliver Hendy; Ann Boija; Jonathan E. Henninger; Charles H. Li; Karel Stejskal; Gen Lin; Katharina Bergauer; Michaela Pagani; Martina Rath; Karl Mechtler; Cosmas D. Arnold; Alexander Stark

Palabras clave: Multidisciplinary.

Pp. 406-413

doi: 10.1038/s41586-022-04773-3

Discovery of non-squalene triterpenes

Hui Tao; Lukas Lauterbach; Guangkai Bian; Rong Chen; Anwei Hou; Takahiro Mori; Shu Cheng; Ben Hu; Li Lu; Xin Mu; Min Li; Naruhiko Adachi; Masato Kawasaki; Toshio Moriya; Toshiya Senda; Xinghuan Wang; Zixin Deng; Ikuro Abe; Jeroen S. Dickschat; Tiangang Liu

<jats:title>Abstract</jats:title><jats:p>All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene<jats:sup>1</jats:sup>. This approach is fundamentally different from the biosynthesis of short-chain (C<jats:sub>10</jats:sub>â€“C<jats:sub>25</jats:sub>) terpenes that are formed from polyisoprenyl diphosphates<jats:sup>2â€“4</jats:sup>. In this study, two fungal chimeric class I TrTSs, <jats:italic>Talaromyces verruculosus</jats:italic> talaropentaene synthase (TvTS) and <jats:italic>Macrophomina phaseolina</jats:italic> macrophomene synthase (MpMS), were characterized. Both enzymes use dimethylallyl diphosphate and isopentenyl diphosphate or hexaprenyl diphosphate as substrates, representing the first examples, to our knowledge, of non-squalene-dependent triterpene biosynthesis. The cyclization mechanisms of TvTS and MpMS and the absolute configurations of their products were investigated in isotopic labelling experiments. Structural analyses of the terpene cyclase domain of TvTS and full-length MpMS provide detailed insights into their catalytic mechanisms. An AlphaFold2-based screening platform was developed to mine a third TrTS, <jats:italic>Colletotrichum gloeosporioides</jats:italic> colleterpenol synthase (CgCS). Our findings identify a new enzymatic mechanism for the biosynthesis of triterpenes and enhance understanding of terpene biosynthesis in nature.</jats:p>

Palabras clave: Multidisciplinary.

Pp. 414-419