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PreprintCited by 4RNA Research and SplicingNuclear Structure and FunctionProtein Structure and Dynamics

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structure of the pre-mRNA leakage 39-kDa protein reveals a single domain of integrated zf-C3HC and Rsm1 modules

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Hashimoto, Hideharu, Ramirez, Daniel H., Lautier, Ophélie, Pawlak, Natalie, Blobel, Günter, Palancade, Benoît, Debler, Erik W.·2022·Scientific Reports
DOI 10.1101/2022.08.11.503642PMC PMC9586977

Preprint — published as 10.1038/s41598-022-22183-3 · Paper page

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Abstract

In Saccharomyces cerevisiae , the pre-mRNA leakage 39-kDa protein ( Sc Pml39) was reported to retain unspliced pre-mRNA prior to export through nuclear pore complexes (NPCs). Pml39 homologs outside the Saccharomycetaceae family are currently unknown, and mechanistic insight into Pml39 function is lacking. Here we determined the crystal structure of Sc Pml39 at 2.5 Å resolution to facilitate the discovery of orthologs beyond Saccharomycetaceae , e.g. in Schizosaccharomyces pombe or human. The crystal structure revealed integrated zf-C3HC and Rsm1 modules, which are tightly associated through a hydrophobic interface to form a single domain. Both zf-C3HC and Rsm1 modules belong to the Zn-containing BIR (Baculovirus IAP repeat)-like super family, with key residues of the canonical BIR domain being conserved. Features unique to the Pml39 modules refer to the spacing between the Zn-coordinating residues, giving rise to a substantially tilted helix aC in the zf-C3HC and Rsm1 modules, and an extra helix αAB’ in the Rsm1 module. Conservation of key residues responsible for its distinct features identifies S. pombe Rsm1 and Homo sapiens NIPA/ZC3HC1 as structural orthologs of Sc Pml39. Based on the recent functional characterization of NIPA/ZC3HC1 as a scaffold protein that stabilizes the nuclear basket of the NPC, our data suggest an analogous function of Sc Pml39 in S. cerevisiae .

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Metadata

Authors
Hashimoto, H., Ramirez, D. H., Lautier, O., Pawlak, N., Blobel, G., Palancade, B., & Debler, E. W.
Affiliations
  • Thomas Jefferson University (US)
  • Howard Hughes Medical Institute (US)
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
Debler, Erik W.
ORCID
Venue
Scientific Reports
Publisher
openRxiv
Published
2022-08-12
Volume
12
Issue
1
Pages
17691-17691
ISSN
2045-2322 (ISSN-L)
DOI
10.1101/2022.08.11.503642
PMC
PMC9586977
OpenAlex
W4307028398
Cited by
4
References
1
Citations by year
2026: 1 · 2025: 2 · 2023: 1
FWCI
0.24
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Scientific Reports (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • The Medicine Forum (submittedVersion, cc-by)
  • HAL (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Howard Hughes Medical Institute (P30 GM124169-01, DE-AC02-05CH11231)
  • U.S. Department of Energy (-AC02-05CH11231, Contract No. DE-AC02-05-CH11231, 05CH11231, P30 GM124169, No. DE-AC02-05-CH11231, DE AC02 05CH11231, GM124169, DE-AC02-)
  • Agence Nationale de la Recherche (ANR18, DE-AC02-05CH11231, ANR-18-CE12-0003)
  • National Institutes of Health (DE-AC02–05CH11231, 1s10od023479-01a1, 1s10od017987-01, P30-GM124169-01, GM124169, CA56036)
  • Office of Science (No. DE-AC02- 05-CH11231, P30 GM124169, DEAC02–05CH11231, AC02-05CH11231, DE-AC02, 05CH11231, P30 GM124169-01, Contract No. DE-AC02-05CH11231)
  • Perelman School of Medicine, University of Pennsylvania
  • National Cancer Institute (S10 OD017987, DE-AC02-05CH11231, P30CA056036)
  • National Institute of General Medical Sciences (DE-AC02-05CH11231, OD017987, GM124169-01, GM124169, P30GM124169)
  • National Institute of Allergy and Infectious Diseases (R21AI154191, R01AI165840)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
nuclear pore complex, protein crystal structure, nuclear basket, Saccharomyces cerevisiae, Schizosaccharomyces pombe, scaffold proteins
MeSH terms
Humans, Nuclear Proteins, RNA Precursors, Saccharomyces cerevisiae, Schizosaccharomyces, Cell Cycle Proteins, Nuclear Pore, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Signal Transducing

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