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Eun Ji Lee, Ji Hae Seo, Ji-Hyeon Park, Tam Thuy Lu Vo, Sunho An, Sung-Jin Bae, Hoang Le, Hye Shin Lee, Hee-Jun Wee, Danbi Lee, Young-Hwa Chung, Jeong A Kim, Myoung-Kuk Jang, Soo Hyung Ryu, Ensil Yu, Se Hwan Jang, Zee Yong Park, Kyu-Won Kim
SAM domain and HD domain containing protein 1 (SAMHD1) is a deoxynucleotide triphosphohydrolase (dNTPase) that inhibits retroviruses by depleting intracellular deoxynucleotide triphosphates (dNTPs) in non-cycling myeloid cells. Although SAMHD1 is expressed ubiquitously throughout the human body, the molecular mechanisms regulating its enzymatic activity and function in non-immune cells are relatively unexplored. Here, we demonstrate that the dNTPase activity of SAMHD1 is regulated by acetylation, which promotes cell cycle progression in cancer cells...
September 15, 2017: Oncotarget
Tam Thuy Lu Vo, Ji-Hyeon Park, Ji Hae Seo, Eun Ji Lee, Hoon Choi, Sung-Jin Bae, Hoang Le, Sunho An, Hye Shin Lee, Hee-Jun Wee, Kyu-Won Kim
Aurora kinase A (AuA) is a prerequisite for centrosome maturation, separation, and mitotic spindle assembly, thus, it is essential for cell cycle regulation. Overexpression of AuA is implicated in poor prognosis of many types of cancer. However, the regulatory mechanisms underlying the functions of AuA are still not fully understood. Here, we report that AuA colocalizes with arrest defective protein 1 (ARD1) acetyltransferase during cell division and cell migration. Additionally, AuA is acetylated by ARD1 at lysine residues at positions 75 and 125...
August 22, 2017: Oncotarget
Tam Thuy Lu Vo, Ji-Hyeon Park, Ji Hae Seo, Eun Ji Lee, Hoon Choi, Sung-Jin Bae, Hoang Le, Sunho An, Hye Shin Lee, Hee-Jun Wee, Kyu-Won Kim
Aurora kinase A (AuA) is a prerequisite for centrosome maturation, separation, and mitotic spindle assembly, thus, it is essential for cell cycle regulation. Overexpression of AuA is implicated in poor prognosis of many types of cancer. However, the regulatory mechanisms underlying the functions of AuA are still not fully understood. Here, we report that AuA colocalizes with arrest defective protein 1 (ARD1) acetyltransferase during cell division and cell migration. Additionally, AuA is acetylated by ARD1 at lysine residues at positions 75 and 125...
July 18, 2017: Oncotarget
J H Pagella, R W Mayes, F J Pérez-Barbería, E R Ørskov
Although the conventional in situ ruminal degradability method is a relevant tool to describe the nutritional value of ruminant feeds, its need for rumen-fistulated animals may impose a restriction on its use when considering animal welfare issues and cost. The aim of the present work was to develop a ruminal degradability technique which avoids using surgically prepared animals. The concept was to orally dose a series of porous bags containing the test feeds at different times before slaughter, when the bags would be removed from the rumen for degradation measurement...
January 2018: Animal: An International Journal of Animal Bioscience
Xu Qian, Xinjian Li, Zhimin Lu
Macroautophagy/autophagy is a cellular defense response to stress conditions and is crucial for cell homeostasis maintenance. However, the precise mechanism underlying autophagy initiation, especially in response to glutamine deprivation and hypoxia, is yet to be explored. We recently discovered that PGK1 (phosphoglycerate kinase 1), a glycolytic enzyme, functions as a protein kinase, phosphorylating BECN1/Beclin 1 to initiate autophagy. Under glutamine deprivation or hypoxia stimulation, PGK1 is acetylated at K388 by NAA10/ARD1 in an MTOR-inhibition-dependent manner, leading to the interaction between PGK1 and BECN1 and the subsequent phosphorylation of BECN1 at S30 by PGK1...
July 3, 2017: Autophagy
Xu Qian, Xinjian Li, Qingsong Cai, Chuanbao Zhang, Qiujing Yu, Yuhui Jiang, Jong-Ho Lee, David Hawke, Yugang Wang, Yan Xia, Yanhua Zheng, Bing-Hua Jiang, David X Liu, Tao Jiang, Zhimin Lu
Autophagy is crucial for maintaining cell homeostasis. However, the precise mechanism underlying autophagy initiation remains to be defined. Here, we demonstrate that glutamine deprivation and hypoxia result in inhibition of mTOR-mediated acetyl-transferase ARD1 S228 phosphorylation, leading to ARD1-dependent phosphoglycerate kinase 1 (PGK1) K388 acetylation and subsequent PGK1-mediated Beclin1 S30 phosphorylation. This phosphorylation enhances ATG14L-associated class III phosphatidylinositol 3-kinase VPS34 activity by increasing the binding of phosphatidylinositol to VPS34...
March 2, 2017: Molecular Cell
Ji Hae Seo, Ji-Hyeon Park, Eun Ji Lee, Tam Thuy Lu Vo, Hoon Choi, Jun Yong Kim, Jae Kyung Jang, Hee-Jun Wee, Hye Shin Lee, Se Hwan Jang, Zee Yong Park, Jaeho Jeong, Kong-Joo Lee, Seung-Hyeon Seok, Jin Young Park, Bong Jin Lee, Mi-Ni Lee, Goo Taeg Oh, Kyu-Won Kim
Heat shock protein (Hsp)70 is a molecular chaperone that maintains protein homoeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. However, the mechanisms by which Hsp70 balances these opposing functions under stress conditions remain unknown. Here, we demonstrate that Hsp70 preferentially facilitates protein refolding after stress, gradually switching to protein degradation via a mechanism dependent on ARD1-mediated Hsp70 acetylation. During the early stress response, Hsp70 is immediately acetylated by ARD1 at K77, and the acetylated Hsp70 binds to the co-chaperone Hop to allow protein refolding...
October 6, 2016: Nature Communications
John S DePaolo, Zehua Wang, Jianhui Guo, Guanyi Zhang, Chiping Qian, Haitao Zhang, Jovanny Zabaleta, Wanguo Liu
Prostate cancer is an androgen receptor (AR)-driven disease and post-translational modification of AR is critical for AR activation. We previously reported that Arrest-defective protein 1 (ARD1) is an oncoprotein in prostate cancer. It acetylates and activates AR to promote prostate tumorigenesis. However, the ARD1-targeted residue within AR and the mechanisms of the acetylation event in prostate tumorigenesis remained unknown. In this study, we show that ARD1 acetylates AR at lysine 618 (K618) in vitro and in vivo...
November 1, 2016: Oncotarget
Enerlyn M Lozada, Zdenek Andrysik, Moying Yin, Nicholas Redilla, Kathryn Rice, Peter J Stambrook
The dual specificity phosphatase Cdc25A is a key regulator of the cell cycle that promotes cell cycle progression by dephosphorylating and activating cyclin-dependent kinases. In response to genotoxicants, Cdc25A undergoes posttranslational modifications which contribute to its proteasome-mediated degradation and consequent cell cycle checkpoint arrest. The most thoroughly studied Cdc25A modification is phosphorylation. We now provide the first evidence that Cdc25A can be acetylated and that it directly interacts with the ARD1 acetyltransferase which acetylates Cdc25A both biochemically and in cultured cells...
April 12, 2016: Oncotarget
Robert S Magin, Zachary M March, Ronen Marmorstein
The N-terminal acetyltransferase NatA is a heterodimeric complex consisting of a catalytic subunit (Naa10/ARD1) and an auxiliary subunit (Naa15). NatA co-translationally acetylates the N termini of a wide variety of nascent polypeptides. In addition, Naa10 can act independently to posttranslationally acetylate a distinct set of substrates, notably actin. Recent structural studies of Naa10 have also revealed the molecular basis for N-terminal acetylation specificity. Surprisingly, recent reports claim that Naa10 may also acetylate lysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kinase, and Runt-related transcription factor 2...
March 4, 2016: Journal of Biological Chemistry
Chao Ma, Chinar Pathak, Sang Jae Lee, Ki-Young Lee, Sun-Bok Jang, Minjoo Nam, Hookang Im, Hye-Jin Yoon, Bong-Jin Lee
The Alba superfamily proteins have been regarded as a conserved group of proteins in archaea and eukarya, which have shown to be important in nucleic acid binding, chromatic organization and gene regulation. These proteins often belong to the N-acetyltransferase (NAT) category (N(α)-acetyltransferases or N(ε)-acetyltransferases) and undergo post-translational modifications. Here, we report the crystal structure of Alba from Thermoplasma volcanium (Tv Alba) at 2.4 Å resolution. The acetylation of Tv Alba was monitored and the N-terminal of Tv Alba has been shown to interact with acetyl coenzyme A (Ac-CoA)...
January 15, 2016: Archives of Biochemistry and Biophysics
Akinori Eiyama, Koji Okamoto
Mitophagy is an evolutionarily conserved autophagy pathway that selectively degrades mitochondria. Although it is well established that this degradation system contributes to mitochondrial quality and quantity control, mechanisms underlying mitophagy remain largely unknown. Here, we report that protein N-terminal acetyltransferase A (NatA), an enzymatic complex composed of the catalytic subunit Ard1 and the adaptor subunit Nat1, is crucial for mitophagy in yeast. NatA is associated with the ribosome via Nat1 and acetylates the second amino acid residues of nascent polypeptides...
October 9, 2015: Journal of Biological Chemistry
Yu-Yung Chang, Chun-Hua Hsu
Nα-acetyltransferases (Nats) possess a wide range of important biological functions. Their structures can vary according to the first two residues of their substrate. However, the mechanisms of substrate recognition and catalysis of Nats are elusive. Here, we present two structure of Sulfolobus solfataricus Ard1 (SsArd1), a member of the NatA family, at 2.13 and 1.84 Å. Both structures contain coenzyme A, while the latter also contains a substrate-derived peptide. Sequential structure-based mutagenesis revealed that mutations of critical residues for CoA binding decreased the binding affinity of SsArd1 by 3 ~ 7-fold...
March 2, 2015: Scientific Reports
Ji Hae Seo, Ji-Hyeon Park, Eun Ji Lee, Kyu-Won Kim
ARD1 is present in various species and has several variants derived from alternative splicing of mRNA. Previously, we reported differential biological functions and cellular distributions of mouse ARD1 (mARD1) variants. However, in comparison to mARD1 variants, human ARD1 (hARD1) variants have been rarely studied. In this study, we characterized a hARD1 variant, hARD1(131) and investigated its cellular activities. hARD1(131) mRNA was isolated from HeLa cells and sequenced. Sequence alignment revealed that, compared to hARD1(235), the most common form of hARD1, the mRNA sequence encoding hARD1131 possesses an altered reading frame due to a 46-bp deletion...
February 2015: International Journal of Oncology
S-H Shin, H Yoon, Y-S Chun, H-W Shin, M-N Lee, G T Oh, J-W Park
Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by recovering antioxidant enzymes inactivated by oxidation. Although its functions have been investigated extensively, little is known about the mechanism by which MSRA is regulated. Arrest defective 1 (ARD1) is an enzyme that catalyzes not only N-terminal acetylation as a cotranslational modification but also lysine acetylation as a posttranslational modification. ARD1, which is expressed in most cell types, is believed to participate in diverse biological processes, but its roles are poorly understood...
2014: Cell Death & Disease
Ji Hae Seo, Ji-Hyeon Park, Eun Ji Lee, Tam Thuy Lu Vo, Hoon Choi, Jae Kyung Jang, Hee-Jun Wee, Bum Ju Ahn, Jong-Ho Cha, Min Wook Shin, Kyu-Won Kim
ARD1 is an acetyltransferase with several variants derived from alternative splicing. Among ARD1 variants, mouse ARD1(225) (mARD1(225)), mouse ARD1(235) (mARD1(235)), and human ARD1(235) (hARD1(235)) have been the most extensively characterized and are known to have different biological functions. In the present study, we demonstrated that mARD1(225), mARD1(235), and hARD1(235) have conserved autoacetylation activities, and that they selectively regulate distinct roles of ARD1 variants in tumorigenesis. Using purified recombinants for ARD1 variants, we found that mARD1(225), mARD1(235), and hARD1(235) undergo similar autoacetylation with the target site conserved at the Lys136 residue...
January 2015: International Journal of Oncology
Di Chen, Jiuli Zhang, Justin Minnerly, Tiffany Kaul, Donald L Riddle, Kailiang Jia
The Caenorhabditis elegans dauer larva is a facultative state of diapause. Mutations affecting dauer signal transduction and morphogenesis have been reported. Of these, most that result in constitutive formation of dauer larvae are temperature-sensitive (ts). The daf-31 mutant was isolated in genetic screens looking for novel and underrepresented classes of mutants that form dauer and dauer-like larvae non-conditionally. Dauer-like larvae are arrested in development and have some, but not all, of the normal dauer characteristics...
October 2014: PLoS Genetics
Ji-Hyeon Park, Ji Hae Seo, Hee-Jun Wee, Tam Thuy Lu Vo, Eun Ji Lee, Hoon Choi, Jong-Ho Cha, Bum Ju Ahn, Min Wook Shin, Sung-Jin Bae, Kyu-Won Kim
Arrest defective 1 (ARD1) is an acetyltransferase that is highly conserved across organisms, from yeasts to humans. The high homology and widespread expression of ARD1 across multiple species and tissues signify that it serves a fundamental role in cells. Human ARD1 (hARD1) has been suggested to be involved in diverse biological processes, and its role in cell proliferation and cancer development has been recently drawing attention. However, the subcellular localization of ARD1 and its relevance to cellular function remain largely unknown...
2014: PloS One
Christopher L Owen, David C Marshall, Kathy B R Hill, Chris Simon
The Pauropsalta generic complex is a large group of cicadas (72 described spp.; >82 undescribed spp.) endemic to Australia. No previous molecular work on deep level relationships within this complex has been conducted, but a recent morphological revision and phylogenetic analysis proposed relationships among the 11 genera. We present here the first comprehensive molecular phylogeny of the complex using five loci (1 mtDNA, 4 nDNA), two of which are from nuclear genes new to cicada systematics. We compare the molecular phylogeny to the morphological phylogeny...
February 2015: Molecular Phylogenetics and Evolution
Chao Ma, Chinar Pathak, Sunbok Jang, Sang Jae Lee, Minjoo Nam, Soon-Jong Kim, Hookang Im, Bong-Jin Lee
Acetylation and deacetylation reactions result in biologically important modifications that are involved in normal cell function and cancer development. These reactions, carried out by protein acetyltransferase enzymes, act by transferring an acetyl group from acetyl-coenzymeA (Ac-CoA) to various substrate proteins. Such protein acetylation remains poorly understood in Archaea, and has been only partially described. Information processing in Archaea has been reported to be similar to that in eukaryotes and distinct from the equivalent bacterial processes...
October 2014: Biochimica et Biophysica Acta
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