J 2021

Localization of METTL16 at the Nuclear Periphery and the Nucleolus Is Cell Cycle-Specific and METTL16 Interacts with Several Nucleolar Proteins

STIXOVÁ, Lenka; Denisa KOMŮRKOVÁ; Alena SVOBODOVÁ KOVAŘÍKOVÁ; Paolo FAGHERAZZI; Eva BÁRTOVÁ et al.

Základní údaje

Originální název

Localization of METTL16 at the Nuclear Periphery and the Nucleolus Is Cell Cycle-Specific and METTL16 Interacts with Several Nucleolar Proteins

Autoři

STIXOVÁ, Lenka; Denisa KOMŮRKOVÁ; Alena SVOBODOVÁ KOVAŘÍKOVÁ; Paolo FAGHERAZZI a Eva BÁRTOVÁ

Vydání

Life, MDPI, 2021, 2075-1729

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 3.253

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/21:00122231

Organizační jednotka

Přírodovědecká fakulta

EID Scopus

Klíčová slova anglicky

METTL16; nucleolus; cell cycle; rDNA; epitranscriptome

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 2. 9. 2021 11:14, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

METTL16 methyltransferase is responsible for the methylation of N-6-adenosine (m(6)A) in several RNAs. In mouse cells, we showed that the nuclear distribution of METTL16 is cell cycle-specific. In the G1/S phases, METTL16 accumulates to the nucleolus, while in the G2 phase, the level of METTL16 increases in the nucleoplasm. In metaphase and anaphase, there is a very low pool of the METTL16 protein, but in telophase, residual METTL16 appears to be associated with the newly formed nuclear lamina. In A-type lamin-depleted cells, we observed a reduction of METTL16 when compared with the wild-type counterpart. However, METTL16 does not interact with A-type and B-type lamins, but interacts with Lamin B Receptor (LBR) and Lap2 alpha. Additionally, Lap2 alpha depletion caused METTL16 downregulation in the nuclear pool. Furthermore, METTL16 interacted with DDB2, a key protein of the nucleotide excision repair (NER), and also with nucleolar proteins, including TCOF, NOLC1, and UBF1/2, but not fibrillarin. From this view, the METTL16 protein may also regulate the transcription of ribosomal genes because we observed that the high level of m(6)A in 18S rRNA appeared in cells with upregulated METTL16.