Evidence map›Paper›PMID 26826708›Full record

ArticleNucleic acids research2016

Identification of LACTB2, a metallo-β-lactamase protein, as a human mitochondrial endoribonuclease.

Shiri Levy, Charles K Allerston, Varda Liveanu, Mouna R Habib, Opher Gileadi, Gadi Schuster

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
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

28 citing papers in PubMed, 47 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Shiri LevyFaculty of Biology, Technion- Israel Institute of Technology, Haifa 32000, Israel.
Charles K AllerstonStructural Genomics Consortium, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK.
Varda LiveanuFaculty of Biology, Technion- Israel Institute of Technology, Haifa 32000, Israel.
Mouna R HabibFaculty of Biology, Technion- Israel Institute of Technology, Haifa 32000, Israel.
Opher GileadiStructural Genomics Consortium, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK opher.gileadi@sgc.ox.ac.uk.
Gadi SchusterFaculty of Biology, Technion- Israel Institute of Technology, Haifa 32000, Israel gadis@tx.technion.ac.il.
Technion – Israel Institute of Technology · ILGenomics England · GBUniversity of Oxford · GB

Funding

Wellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

Post-transcriptional control of mitochondrial gene expression, including the processing and generation of mature transcripts as well as their degradation, is a key regulatory step in gene expression in human mitochondria. Consequently, identification of the proteins responsible for RNA processing and degradation in this organelle is of great importance. The metallo-β-lactamase (MBL) is a candidate protein family that includes ribo- and deoxyribonucleases. In this study, we discovered a function for LACTB2, an orphan MBL protein found in mammalian mitochondria. Solving its crystal structure revealed almost perfect alignment of the MBL domain with CPSF73, as well as to other ribonucleases of the MBL superfamily. Recombinant human LACTB2 displayed robust endoribonuclease activity on ssRNA with a preference for cleavage after purine-pyrimidine sequences. Mutational analysis identified an extended RNA-binding site. Knockdown of LACTB2 in cultured cells caused a moderate but significant accumulation of many mitochondrial transcripts, and its overexpression led to the opposite effect. Furthermore, manipulation of LACTB2 expression resulted in cellular morphological deformation and cell death. Together, this study discovered that LACTB2 is an endoribonuclease that is involved in the turnover of mitochondrial RNA, and is essential for mitochondrial function in human cells.

Indexed as

beta-LactamasesBinding SitesCrystallography, X-RayEndoribonucleasesHumansMetalloproteinsMitochondriaProtein Structure, TertiaryRNARNA-Binding ProteinsRNA, Mitochondrialbeta-LactamasesEndoribonucleasesLACTB2 protein, humanMetalloproteinsRNARNA-Binding ProteinsRNA, Mitochondrial

Identifiers

PMID26826708
PMCPMC4770246
OpenAlexW2257954678

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.