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Peter Askjaer

Researcher at Pablo de Olavide University

Publications -  70
Citations -  3766

Peter Askjaer is an academic researcher from Pablo de Olavide University. The author has contributed to research in topics: Caenorhabditis elegans & Chromatin. The author has an hindex of 26, co-authored 61 publications receiving 3244 citations. Previous affiliations of Peter Askjaer include Spanish National Research Council & Aarhus University.

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Step-wise methylation of histone H3K9 positions heterochromatin at the nuclear periphery.

TL;DR: Analysis of histone methyltransferases showed that elimination of two HMTs, MET-2 and SET-25, mimics the loss of SAM synthetase, abrogating the perinuclear attachment of heterochromatic transgenes and of native chromosomal arms rich in histone H3 lysine 9 methylation.
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MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly

TL;DR: Using in vitro NE assembly, it is shown that the vertebrate homologue of MEL‐28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly and is suggested that M EL‐28 acts as a seeding point for NPC assembly.
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The Specificity of the CRM1-Rev Nuclear Export Signal Interaction Is Mediated by RanGTP*

TL;DR: The data are consistent with a model in which CRM1 is the nuclear export receptor for the Rev-RRE ribonucleoprotein complex and that RanGTP binds to a preformed Rev-CRM1 complex and specifies a functional interaction with the NES.
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RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase.

TL;DR: Using a quantitativeCRM1-NES cargo binding assay, significant differences in affinity for CRM1 among natural NESs are demonstrated, suggesting that the steady-state nucleocytoplasmic distribution of shuttling proteins could be determined by the relative strengths of their NESs.
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RanGTP mediates nuclear pore complex assembly

TL;DR: RanGTP production is required to dissociate nucleoporins Nup107, Nup153 and Nup358 from Importin β, to target them to chromatin and to induce association between separate NPC subcomplexes, and a mechanism for the spatial restriction of NPC assembly to the surface of chromatin is suggested.