PuSH - Publication Server of Helmholtz Zentrum München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Wagner, A. ; Hofmeister, O. ; Rolland, S.G.* ; Maiser, A.* ; Aasumets, K.* ; Schmitt, S.* ; Schorpp, K.K. ; Feuchtinger, A. ; Hadian, K. ; Schneider, S.* ; Zischka, H. ; Leonhardt, H.* ; Conradt, B.* ; Gerhold, J.M.* ; Wolf, A.

Mitochondrial Alkbh1 localizes to mtRNA granules and its knockdown induces the mitochondrial UPR in humans and C. elegans.

J. Cell Sci. 132:jcs223891 (2019)
Publ. Version/Full Text DOI PMC
Closed
Open Access Green as soon as Postprint is submitted to ZB.
The Fe(II) and 2-oxoglutarate-dependent oxygenase Alkb homologue 1 (Alkbh1) has been shown to act on a wide range of substrates, like DNA, tRNA and histones. Thereby different enzymatic activities have been identified including, among others, demethylation of N3-methylcytosine (m(3)C) in RNA- and single-stranded DNA oligonucleotides, demethylation of N-1-methyladenosine (m1A) in tRNA or formation of 5-formyl cytosine (f(5)C) in tRNA. In accordance with the different substrates, Alkbh1 has also been proposed to reside in distinct cellular compartments in human and mouse cells, including the nucleus, cytoplasm and mitochondria. Here, we describe further evidence for a role of human Alkbh1 in regulation of mitochondrial protein biogenesis, including visualizing localization of Alkbh1 into mitochondrial RNA granules with super-resolution 3D SIM-microscopy. Electron microscopy and high-resolution respirometry analyses revealed an impact of Alkbh1 level on mitochondrial respiration, but not on mitochondrial structure. Downregulation of Alkbh1 impacts cell growth in HeLa cells and delays development in Caenorhabditis elegans, where the mitochondrial role of Alkbh1 seems to be conserved. Alkbh1 knockdown, but not Alkbh7 knockdown, triggers the mitochondrial unfolded protein response (UPRmt) in C. elegans.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
4.517
1.006
10
10
Tags
Annotations
Special Publikation
Hide on homepage

Edit extra information
Edit own tags
Private
Edit own annotation
Private
Hide on publication lists
on hompage
Mark as special
publikation
Publication type Article: Journal article
Document type Scientific Article
Keywords Rna Modifications ; Mitochondrial Unfolded Protein Response ; Fe(ii) And 2-oxoglutarate Dependent Oxygenase ; Jumonji-domain-containing Enzyme ; Rna Granules ; Mitochondrial Structure; Dna-repair Enzymes; Wobble Position; Stress-response; Protein; Dioxygenase; Cells; N-6-adenine; Methylation; Mechanisms; Alkylation
Language english
Publication Year 2019
HGF-reported in Year 2019
ISSN (print) / ISBN 0021-9533
e-ISSN 1477-9137
Journal Journal of Cell Science
Quellenangaben Volume: 132, Issue: 19, Pages: , Article Number: jcs223891 Supplement: ,
Publisher Company of Biologists
Publishing Place Cambridge
Reviewing status Peer reviewed
Institute(s) Institute of Molecular Toxicology and Pharmacology (TOX)
Research Unit Analytical Pathology (AAP)
CF Pathology & Tissue Analytics (CF-PTA)
POF-Topic(s) 30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
30203 - Molecular Targets and Therapies
30205 - Bioengineering and Digital Health
30505 - New Technologies for Biomedical Discoveries
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-552500-001
G-505293-001
G-500390-001
G-505200-003
A-630600-001
DOI 10.1242/jcs.223891
WOS ID WOS:000490938000004
Scopus ID 85072849394
PubMed ID 31434717
Erfassungsdatum 2019-09-25
[➜Report correction]