Dataset Information

Identification of METTL5 interaction partners

ABSTRACT: METTL5 is an RNA methyltransferase whose stability was noted to be poor when expressed in both mammalian and bacterial expression systems. To determine if METTL5 has an endogenous stabilizing binding partner, FLAG-tagged METTL5 was expressed in Freestyle 293 cells and pulled down with anti-FLAG-M2 antibody-coupled magnetic beads. Bound proteins were fractionated by SDS-PAGE, and bands of interest were cut out for proteomics analysis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Sigrid Nachtergaele

LAB HEAD: Sigrid Nachtergaele

PROVIDER: PXD029574 | Pride | 2022-01-27

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	MSB39527A.raw	Raw
	MSB39527A__F150922_.mzid.gz	Mzid
	MSB39527A__F150922_.mzid_MSB39527A__F150922_.MGF	Mzid
	MSB39528A.raw	Raw
	MSB39528A__F150923_.mzid.gz	Mzid

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Publications

The METTL5-TRMT112 N6-methyladenosine methyltransferase complex regulates mRNA translation via 18S rRNA methylation.

Sepich-Poore Caraline C Zheng Zhong Z Schmitt Emily E Wen Kailong K Zhang Zijie Scott ZS Cui Xiao-Long XL Dai Qing Q Zhu Allen C AC Zhang Linda L Sanchez Castillo Arantxa A Tan Haiyan H Peng Junmin J Zhuang Xiaoxi X He Chuan C Nachtergaele Sigrid S

The Journal of biological chemistry 20220114 3

Ribosomal RNAs (rRNAs) have long been known to carry chemical modifications, including 2'O-methylation, pseudouridylation, N6-methyladenosine (m6A), and N6,6-dimethyladenosine. While the functions of many of these modifications are unclear, some are highly conserved and occur in regions of the ribosome critical for mRNA decoding. Both 28S rRNA and 18S rRNA carry single m6A sites, and while the methyltransferase ZCCHC4 has been identified as the enzyme ...[more]

PMID: 35033535

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Project description:Cellular senescence due to telomere dysfunction has been hypothesized to play a role in age-associated diseases including idiopathic pulmonary fibrosis (IPF). It has been postulated that paracrine mediators originating from senescent alveolar epithelia signal to surrounding mesenchymal cells and contribute to disease pathogenesis. However, murine models of telomere-induced alveolar epithelial senescence fail to display the canonical senescence-associated secretory phenotype (SASP) that is observed in senescent human cells. In an effort to understand human-specific responses to telomere dysfunction, we modelled telomere dysfunction-induced senescence in a human alveolar epithelial cell line. We hypothesized that this system would enable us to probe for differences in transcriptional and proteomic senescence pathways in vitro and to identify novel secreted protein (secretome) changes that potentially contribute to the pathogenesis of IPF. Following induction of telomere dysfunction, a robust senescence phenotype was observed. RNA-Seq analysis of the senescent cells revealed the SASP and comparisons to previous murine data highlighted species-specific responses to telomere dysfunction. We then conducted a proteomic analysis of the senescent cells using a novel biotin ligase capable of labeling secreted proteins. Candidate biomarkers selected from our transcriptional and secretome data were then evaluated in IPF and control patient plasma. Four novel proteins were found to be differentially expressed between the patient groups: stanniocalcin-1, contactin-1, tenascin C, and total inhibin. Our data show that human telomere-induced, alveolar epithelial senescence results in a transcriptional SASP that is distinct from that seen in analogous murine cells. Our findings suggest that studies in animal models should be carefully validated given the species-specific responses to telomere dysfunction. We also describe a pragmatic approach for the study of the consequences of telomere-induced alveolar epithelial cell senescence in humans.

Dataset Information

Identification of METTL5 interaction partners

Dataset's files

Publications

The METTL5-TRMT112 N<sup>6</sup>-methyladenosine methyltransferase complex regulates mRNA translation via 18S rRNA methylation.

Similar Datasets

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