Literature DB >> 35098449

Solution NMR backbone assignments of disordered Olduvai protein domain CON1 employing Hα-detected experiments.

Natasia Paukovich1, Morkos A Henen1,2, Alya Hussain1, Aaron Issaian1, James M Sikela1, Kirk C Hansen1, Beat Vögeli3.   

Abstract

Olduvai protein domains, encoded by the NBPF gene family, are responsible for the largest increase in copy number of any protein-coding region in the human genome. This has spawned various genetics studies which have linked these domains to human brain development and divergence from our primate ancestors, as well as currently relevant cognitive diseases such as schizophrenia and autism spectrum disorder (ASD). There are six separate Olduvai domains which together form the majority of the various protein products of the NBPF genes. The six domains include three conserved domains (CON1-3), and three human-lineage-specific domains (HLS1-3) which occur in triplet. Here, we present the solution nuclear magnetic resonance backbone assignments for the CON1 domain, which has been linked to the severity of ASD. The data confirm that CON1 is an intrinsically disordered protein (IDP). Additionally, we use innovative Hα-detected experiments which allow us to not only assign the Hα atoms and N atoms of proline residues, but also to assign residues where HN-experiments suffered from peak overlap or broadening.
© 2022. The Author(s), under exclusive licence to Springer Nature B.V.

Entities:  

Keywords:  Autism; Backbone chemical shift assignment; DUF1220; IDP; Olduvai domain

Mesh:

Substances:

Year:  2022        PMID: 35098449      PMCID: PMC9202364          DOI: 10.1007/s12104-022-10068-5

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.731


  19 in total

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5.  Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling.

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Journal:  J Biomol NMR       Date:  2012-02-14       Impact factor: 2.835

6.  A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

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7.  Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains.

Authors:  Aaron Issaian; Lauren Schmitt; Alexandra Born; Parker J Nichols; James Sikela; Kirk Hansen; Beat Vögeli; Morkos A Henen
Journal:  Biomol NMR Assign       Date:  2019-07-01       Impact factor: 0.746

8.  The CCPN data model for NMR spectroscopy: development of a software pipeline.

Authors:  Wim F Vranken; Wayne Boucher; Tim J Stevens; Rasmus H Fogh; Anne Pajon; Miguel Llinas; Eldon L Ulrich; John L Markley; John Ionides; Ernest D Laue
Journal:  Proteins       Date:  2005-06-01

9.  CheSPI: chemical shift secondary structure population inference.

Authors:  Jakob Toudahl Nielsen; Frans A A Mulder
Journal:  J Biomol NMR       Date:  2021-06-19       Impact factor: 2.835

10.  NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy.

Authors:  Woonghee Lee; Marco Tonelli; John L Markley
Journal:  Bioinformatics       Date:  2014-12-12       Impact factor: 6.937

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