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Gene regulation of mammalian long non-coding RNA
Springer-Verlag 2018 Molecular genetics and genomics Vol.293 No.1
<P>RNA polymerase II (Pol II) transcribes two classes of RNAs, protein-coding and non-protein-coding (ncRNA) genes. ncRNAs are also synthesized by RNA polymerases I and III (Pol I and III). In humans, the number of ncRNA genes exceeds more than twice that of protein-coding genes. However, the history of studying Pol II-synthesized ncRNA is relatively short. Since early 2000s, important biological and pathological functions of these ncRNA genes have begun to be discovered and intensively studied. And transcription mechanisms of long non-coding RNA (lncRNA) have been recently reported. Transcription of lncRNAs utilizes some transcription factors and mechanisms shared in that of protein-coding genes. In addition, tissue specificity in lncRNA gene expression has been shown. LncRNAs play essential roles in regulating the expression of neighboring or distal genes through different mechanisms. This leads to the implication of lncRNAs in a wide variety of biological pathways and pathological development. In this review, the newly discovered transcription mechanisms, characteristics, and functions of lncRNA are discussed.</P>
RNA polymerase II pausing and transcriptional regulation of the <i>HSP70</i> expression
Elsevier 2017 European journal of cell biology Vol.96 No.8
<P><B>Abstract</B></P> <P>Heat-shock proteins (HSPs) belong to the chaperone protein family whose expression is induced by different stresses including heat-shock. In response to the extracellular or intrinsic stimuli and stresses, HSPs play important roles in the maintenance of cellular homeostasis. HSP70, a major HSP protein (molecular weight, 70 KDa), regulates diverse cellular pathways including protein quality control, translation, immune response, and cancer survival. As a critical cellular defense system to minimize damages from cellular stresses, <I>HSP70</I> expression and transcriptional activation are rapidly regulated, mainly through the action of a transcription activator, Heat shock factor 1 (HSF1). Eukaryotic <I>HSP70</I> genes are well-characterized; they utilize a transcriptional mechanism termed as RNA polymerase II (Pol II) promoter-proximal pausing. Pol II promoter-proximal pausing enables synchronized gene expression in a number of mammalian protein-coding and non-protein coding genes upon the reception of gene activating signals. In particular, <I>Drosophila</I> and human <I>HSP70</I> genes serve as a <I>bona fide</I> model system to understand the mechanisms of Pol II pausing and pause release. In this review, we will discuss <I>HSP70</I> transcription and the newly discovered mechanisms that regulate <I>HSP70</I> gene expression.</P>
Triamterene induces autophagic degradation of lysosome by exacerbating lysosomal integrity
박나연,Doo Sin Jo,Yong Hwan Kim,Ji-Eun Bae,Joon Bum Kim,Hyun Jun Park,Ji Yeon Choi,Ha Jung Lee,Jeong Ho Chang,Heeyoun Bunch,Hong Bae Jeon,Yong-Keun Jung,Dong-Hyung Cho 대한약학회 2021 Archives of Pharmacal Research Vol.44 No.6
The maintenance of lysosomal integrity is essentialfor lysosome function and cell fate. Damaged lysosomesare degraded by lysosomal autophagy, lysophagy. Themechanism underlying lysophagy remains largely unknown;this study aimed to contribute to the understanding of thistopic. A cell-based screening system was used to identifynovel lysophagy modulators. Triamterene (6-phenylpteridine-2,4,7-triamine) was identifi ed as one of the most potentlysophagy inducers from the screening process. We foundthat triamterene causes lysosomal rupture without aff ectingother cellular organelles and increases autophagy fl uxin HepG2 cells. Damaged lysosomes in triamterene-treatedcells were removed by autophagy-mediated pathway, whichwas inhibited by depletion of the autophagy regulator, ATG5or SQSTM1. In addition, treatment of triamterene decreased the integrity of lysosome and cell viability, which were rescuedby removing the triamterene treatment in HepG2 cells. Hence, our data suggest that triamterene is a novel lysophagyinducer through the disruption of lysosomal integrity.
Ju-Ri Woo,Doo-Ho Choi,Muhammed Taofiq Hamza,Kyung-Oh Doh,Chang-Yoon Lee,Yeon-Sik Choo,Sangman Lee,Jong-Guk Kim,Heeyoun Bunch,Young-Bae Seu 한국균학회 2022 Mycobiology Vol.50 No.5
Regulation of proper gene expression is important for cellular and organismal survival, main- tenance, and growth. Abnormal gene expression, even for a single critical gene, can thwart cellular integrity and normal physiology to cause diseases, aging, and death. Therefore, gene expression profiling serves as a powerful tool to understand the pathology of diseases and to cure them. In this study, the difference in gene expression in Flammulina velutipes was compared between the wild type (WT) mushroom and the mutant one with clogging phe- nomenon. Differentially expressed transcripts were screened to identify the candidate genes responsible for the mutant phenotype using the DNA microarray analysis. A total of 88 genes including 60 upregulated and 28 downregulated genes were validated using the real- time quantitative PCR analysis. In addition, proteomic differences between the WT and mutant mushroom were analyzed using two–dimensional gel electrophoresis and matrix- assisted laser desorption/ionization-time of flight (MALDI-TOF). Interestingly, the genes iden- tified by these genomic and proteomic analyses were involved in stress response, transla- tion, and energy/sugar metabolism, including HSP70, elongation factor 2, and pyruvate kinase. Together, our data suggest that the aberrant expression of these genes attributes to the mutant clogging phenotype. We propose that these genes can be targeted to foster normal growth in F. velutipes.