Evidence map›Paper›PMID 38352541›Full record

ArticlebioRxiv : the preprint server for biology2024

Functional Analysis of the Zinc Finger Modules of the

Tucker J Carrocci, Samuel DeMario, Kevin He, Natalie J Zeps, Cade T Harkner, Guillaume Chanfreau, Aaron A Hoskins

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Tucker J CarrocciDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Samuel DeMarioDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Kevin HeDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Natalie J ZepsDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Cade T HarknerDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Guillaume ChanfreauDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.ORCID 0000-0002-2505-1950
Aaron A HoskinsDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.ORCID 0000-0002-9777-519X
University of Wisconsin–Madison · USUniversity of California, Los Angeles · US

Funding

The Control of Gene Expression by Eukaryotic RibonucleasesR35GM130370 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Guillaume F Chanfreau · 2019 to 2026
$3.3M
Mechanisms of Spliceosome Assembly and RegulationR35GM136261 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Aaron Andrew Hoskins · 2020 to 2026
$3.2M
NIGMS NIH HHS R35 GM130370NIGMS NIH HHS R35 GM136261
6 · The paper itself

Abstract

Identification of splice sites is a critical step in pre-mRNA splicing since definition of the exon/intron boundaries controls what nucleotides are incorporated into mature mRNAs. The intron boundary with the upstream exon is initially identified through interactions with the U1 snRNP. This involves both base pairing between the U1 snRNA and the pre-mRNA as well as snRNP proteins interacting with the 5' splice site/snRNA duplex. In yeast, this duplex is buttressed by two conserved protein factors, Yhc1 and Luc7. Luc7 has three human paralogs (LUC7L, LUC7L2, and LUC7L3) which play roles in alternative splicing. What domains of these paralogs promote splicing at particular sites is not yet clear. Here, we humanized the zinc finger domains of the yeast Luc7 protein in order to understand their roles in splice site selection using reporter assays, transcriptome analysis, and genetic interactions. While we were unable to determine a function for the first zinc finger domain, humanization of the second zinc finger domain to mirror that found in LUC7L or LUC7L2 resulted in altered usage of nonconsensus 5' splice sites. In contrast, the corresponding zinc finger domain of LUC7L3 could not support yeast viability. Further, humanization of Luc7 can suppress mutation of the ATPase Prp28, which is involved in U1 release and exchange for U6 at the 5' splice site. Our work reveals a role for the second zinc finger of Luc7 in splice site selection and suggests that different zinc finger domains may have different ATPase requirements for release by Prp28.

Indexed as

Luc7RNAsnRNPSpliceosomeSplicing

Identifiers

PMID38352541
PMCPMC10862913
OpenAlexW4391537739

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.