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RISS 인기검색어
- 검색키워드
- 저자 : Anton Gartner (검색결과 3 건)
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Sirtuin/Sir2 Phylogeny, Evolutionary Considerations and Structural Conservation
Sebastian Greiss,Anton Gartner 한국분자세포생물학회 2009 Molecules and cells Vol.28 No.5
The sirtuins are a protein family named after the first identified member, S. cerevisiae Sir2p. Sirtuins are protein deacetylases whose activity is dependent on NAD+ as a cosubstrate. They are structurally defined by two central domains that together form a highly conserved catalytic center, which catalyzes the transfer of an acetyl moiety from acetyllysine to NAD+, yielding nicotinamide, the unique metabolite O-acetyl-ADP-ribose and deacetylated lysine. One or more sirtuins are present in virtually all species from bacteria to mammals. Here we describe a phylogenetic analysis of sirtuins. Based on their phylogenetic relationship, sirtuins can be grouped into over a dozen classes and subclasses. Humans, like most vertebrates, have seven sirtuins: SIRT1-SIRT7. These function in diverse cellular pathways, regulating transcriptional repression, aging, metabolism, DNA damage responses and apoptosis. We show that these seven sirtuins arose early during animal evolution. Conserved residues cluster around the catalytic center of known sirtuin family members.
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Lee, Se-Jin,Gartner, Anton,Hyun, Moonjung,Ahn, Byungchan,Koo, Hyeon-Sook Public Library of Science 2010 PLoS genetics Vol.6 No.1
<▼1><P>WRN-1 is the <I>Caenorhabditis elegans</I> homolog of the human Werner syndrome protein, a RecQ helicase, mutations of which are associated with premature aging and increased genome instability. Relatively little is known as to how WRN-1 functions in DNA repair and DNA damage signaling. Here, we take advantage of the genetic and cytological approaches in <I>C. elegans</I> to dissect the epistatic relationship of WRN-1 in various DNA damage checkpoint pathways. We found that WRN-1 is required for CHK1 phosphorylation induced by DNA replication inhibition, but not by UV radiation. Furthermore, WRN-1 influences the RPA-1 focus formation, suggesting that WRN-1 functions in the same step or upstream of RPA-1 in the DNA replication checkpoint pathway. In response to ionizing radiation, RPA-1 focus formation and nuclear localization of ATM depend on WRN-1 and MRE-11. We conclude that <I>C. elegans</I> WRN-1 participates in the initial stages of checkpoint activation induced by DNA replication inhibition and ionizing radiation. These functions of WRN-1 in upstream DNA damage signaling are likely to be conserved, but might be cryptic in human systems due to functional redundancy.</P></▼1><▼2><P><B>Author Summary</B></P><P>Werner syndrome is a premature aging syndrome associated with genomic instability. The protein linked to Werner syndrome, WRN, has both helicase and exonuclease activities and is thought to be involved in DNA repair, including the resolution of replication fork arrest as well as in telomere maintenance. However, no definite and detailed role of the protein has been elucidated in vivo. We take advantage of the <I>Caenorhabditis elegans</I> germ cell system to explore DNA damage response defects associated with WRN, and we focus particularly on the role of <I>wrn</I> in the cell cycle checkpoint in response to DNA replication blockage and ionizing radiation (IR). We show that WRN functions together with RPA upstream of <I>C. elegans</I> ATR in the intra S-phase checkpoint pathway, and upstream of <I>C. elegans</I> ATM and RPA in the cell cycle arrest pathway triggered by IR–induced double-strand DNA breaks. These functions of WRN in upstream DNA damage signaling are likely to be conserved, but not obvious in human systems due to functional redundancy.</P></▼2>
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Lee, Hyojin,Cho, Jeong Soo,Lambacher, Nils,Lee, Jieun,Lee, Se-Jin,Lee, Tae Hoon,Gartner, Anton,Koo, Hyeon-Sook American Society for Biochemistry and Molecular Bi 2008 The Journal of biological chemistry Vol.283 No.22
<P>AAK-2 is one of two alpha isoforms of the AMP-activated protein kinase in Caenorhabditis elegans and is involved in life span maintenance, stress responses, and germ cell cycle arrest upon dauer entry. We found that AAK-2 was phosphorylated at threonine 243 in response to paraquat treatment and that this phosphorylation depends on PAR-4, the C. elegans LKB1 homologue. Both aak-2 mutation and par-4 knockdown increased the sensitivity of C. elegans worms to paraquat, and the double deficiency did not further increase sensitivity, indicating that aak-2 and par-4 act in a linear pathway. Both mutations also slowed body bending during locomotion and failed to reduce head oscillation in response to anterior touch. Consistent with this abnormal motility and behavioral response, expression of the AAK-2::green fluorescent protein fusion protein was observed in the ventral cord, some neurons, body wall muscle, pharynx, vulva, somatic gonad, and excretory cell. Our study suggests that AMPK can influence the behavior of C. elegans worms in addition to its well known function in metabolic control.</P>
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