PUM3

Last update 08 May 2025

Basic Info

Synonyms

cPERP-C, HA-8, HBV X-transactivated gene 5 protein

+ [12]

Introduction

Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence specificity (PubMed:25512524). Involved in development of the eye and of primordial germ cells (By similarity).

100 Clinical Results associated with PUM3

100 Translational Medicine associated with PUM3

0 Patents (Medical) associated with PUM3

Literatures (Medical) associated with PUM3

01 Jan 2025·Bioresource Technology

Identification of xenobiotic response element family transcription regulator SadR from sulfonamides-degrading strain Microbacterium sp. HA-8 and construction of biosensor to detect sulfonamides

Article

Author: Liu, Hongfei ; Hong, Qing ; Pan, Kaihua ; Wang, Fang ; Hu, Junqiang ; Li, Qian ; Huang, Yanni ; Zhu, Qian ; Zhu, Weihao ; Wang, Changchang ; Jiang, Mingli ; Zhang, Mingliang

Deciphering the regulatory mechanisms of sulfonamides (SAs) metabolism will contribute to a deeper understanding of SAs degradation in the environment. In this study, a SAs-degrading strain Microbacterium sp. HA-8 harboring a highly conserved SAs-degrading genes sadABC was isolated. SadR was a newly discovered regulator, belonging to xenobiotic response element (XRE) family, which negatively regulated the transcription of sadAB genes. Specifically, SadR bound to the sadA promoter region to repress the expression of sadAB genes. While, SAs prevented SadR from binding to sadA promoter to induce the expression of sadAB genes. Then, a whole-cell biosensor, Escherichia coli DH5α/pSRmCherry was constructed to detect SAs. The dose-dependent fluorescence of the biosensor exhibited a good fit to Hill equation. In summary, this study revealed the regulatory mechanism of SAs degradation in strain HA-8 and developed an innovative biosensor technique for detecting SAs, holding promise for future applications in environmental monitoring.

10 Nov 2023·Nucleic Acids Research

Yeast ribosome biogenesis factors Puf6 and Nog2 and ribosomal proteins uL2 and eL43 act in concert to facilitate the release of nascent large ribosomal subunits from the nucleolus

Article

Author: Hedayati, Stefanie ; Oualline, Grace ; Micic, Jelena ; Fitzgerald, Fiona ; LaPeruta, Amber J ; Kim, David ; Woolford, John L

AbstractLarge ribosomal subunit precursors (pre-LSUs) are primarily synthesized in the nucleolus. At an undetermined step in their assembly, they are released into the nucleoplasm. Structural models of yeast pre-LSUs at various stages of assembly have been collected using cryo-EM. However, which cryo-EM model is closest to the final nucleolar intermediate of the LSU has yet to be determined. To elucidate the mechanisms of the release of pre-LSUs from the nucleolus, we assayed effects of depleting or knocking out two yeast ribosome biogenesis factors (RiBi factors), Puf6 and Nog2, and two ribosomal proteins, uL2 and eL43. These proteins function during or stabilize onto pre-LSUs between the late nucleolar stages to early nucleoplasmic stages of ribosome biogenesis. By characterizing the phenotype of these four mutants, we determined that a particle that is intermediate between the cryo-EM model State NE1 and State NE2 likely represents the final nucleolar assembly intermediate of the LSU. We conclude that the release of the RiBi factors Nip7, Nop2 and Spb1 and the subsequent stabilization of rRNA domains IV and V may be key triggers for the release of pre-LSUs from the nucleolus.

01 Aug 2023·Zygote

Pum3is dispensable for mouse oocyte maturation and embryo developmentin vitro

Article

Author: Huang, Wei ; Zhao, TingTing ; Lin, Kaibo

SummaryPumilio3(Pum3), an evolutionarily distant homologue of the classical RNA-binding protein PUF (PUMILIO and FBF) family member, is also involved in the process of RNA metabolism through post-transcriptional regulation. However, the functions ofPum3in mouse oocyte maturation and preimplantation embryonic development have not been elucidated. By comparing RNA levels in different tissues, we found thatPum3was widely expressed in multiple tissues, but moderately predominant in the ovary. Histochemical staining suggested that the PUM3 protein exhibits positive signals in oocytes, granulosa cells and theca cells of different follicle stages. Oocyte immunofluorescence results showed a slightly higher level of PUM3 protein in metaphase II compared with the germinal vesicle (GV) stage. After knockdown ofPum3in GV oocytes using siRNA injection (siPUM3), no obvious defect was observed in the processes of GV breakdown and polar body extrusion duringin vitromaturation (IVM) for thesiPum3oocytes. Compared with the control group, thesiPUM3group displayed no significant abnormality in the cleavage and blastocyst formation rate of these fertilized oocytes. Therefore, we can conclude that depletion ofPum3does not affect mouse oocyte maturation and early embryonic developmentin vitro.

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