関: terminal deoxynucleotide transferase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/21 06:19:47」(JST)

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Nucleotidyltransferases are transferase enzymes of phosphorus-containing groups, e.g., substituents of nucleotidylic acids or simply nucleoside monophosphates. The general reaction of transferring a nucleoside monophosphate moiety from A to B, can be written as:

A-P-N + B A + B-P-N

For example, in the case of polymerases, A is pyrophosphate and B is the nascent polynucleotide. They are classified under EC number 2.7.7 and they can be categorised into:

Uridylyltransferases, which transfer uridylyl- groups
Adenylyltransferases, which transfer adenylyl- groups
Guanylyltransferases, which transfer guanylyl- groups
Cytitidylyltransferases, which transfer cytidylyl- groups
Thymidylyltransferases, which transfer thymidylyl- groups

Role in DNA repair mechanisms

Nucleotidyl transferase is a component of the repair pathway for single nucleotide base excision repair. This repair mechanism begins when a single nucleotide is recognized by DNA glycosylase as incorrectly matched or has been mutated in some way (UV light, chemical mutagen, etc.), and is removed. Later, a nucleotidyl tranferase is used to fill in the gap with the correct base, using the template strand as the reference. ^[1]

References

^ Yuan Liu, Rajendra Prasad, William A. Beard, Padmini S. Kedar, Esther W. Hou, David D. Shock, and Samuel H. Wilson (May 4, 2007). "Coordination of Steps in Single-nucleotide Base Excision Repair Mediated by Apurinic/Apyrimidinic Endonuclease 1 and DNA Polymerase β" (PDF). Journal of Biological Chemistry 282 (18): 13532–13541. doi:10.1074/jbc.M611295200. PMC 2366199. PMID 17355977. The enzymes and accessory factors involved in the BER subpathways in mammalian cells have received considerable attention. As summarized above, five distinct enzymatic reaction are involved during SN-BER. These are 1) removal of a modified base by a lesion-specific monofunctional DNA N-glycosylase, 2) 5'-incision of the abasic site by a hydrolytic strand incision enzyme, 3) DNA synthesis by a nucleotidyltransferase, 4) removal of the 5'-dRP group by a'-elimination reaction, and 5) nick sealing by DNA ligase (36, 37)

External links

Nucleotidyltransferases at the US National Library of Medicine Medical Subject Headings (MeSH)

Molecular and Cellular Biology portal

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English Journal

Identification of the Novel Lincosamide Resistance Gene lnu(E) Truncated by ISEnfa5-cfr-ISEnfa5 Insertion in Streptococcus suis: De Novo Synthesis and Confirmation of Functional Activity in Staphylococcus aureus.

Zhao Q1, Wendlandt S, Li H, Li J, Wu C, Shen J, Schwarz S, Wang Y.Author information 1Beijing Key Laboratory of Detection Technology for Animal-Derived Food Safety, College of Veterinary Medicine, China Agricultural University, Beijing, People's Republic of China.AbstractThe novel lincosamide resistance gene lnu(E), truncated by insertion of an ISEnfa5-cfr-ISEnfa5 segment, was identified in Streptococcus suis. The gene lnu(E) encodes a 173-amino-acid protein with ≤69.4% identity to other lincosamide nucleotidyltransferases. The lnu(E) gene and its promoter region were de novo synthesized, and Staphylococcus aureus RN4220 carrying a shuttle vector with the cloned lnu(E) gene showed a 16-fold increase in the lincomycin MIC. Mass spectrometry experiments demonstrated that Lnu(E) catalyzed the nucleotidylation of lincomycin.
Antimicrobial agents and chemotherapy.Antimicrob Agents Chemother.2014 Mar;58(3):1785-8. doi: 10.1128/AAC.02007-13. Epub 2013 Dec 23.
The novel lincosamide resistance gene lnu(E), truncated by insertion of an ISEnfa5-cfr-ISEnfa5 segment, was identified in Streptococcus suis. The gene lnu(E) encodes a 173-amino-acid protein with ≤69.4% identity to other lincosamide nucleotidyltransferases. The lnu(E) gene and its promoter region
PMID 24366733

Clinical and epidemiological characteristics of a fatal case of avian influenza A H10N8 virus infection: a descriptive study.

Chen H1, Yuan H2, Gao R3, Zhang J4, Wang D3, Xiong Y2, Fan G1, Yang F5, Li X3, Zhou J3, Zou S3, Yang L3, Chen T3, Dong L3, Bo H3, Zhao X3, Zhang Y3, Lan Y3, Bai T3, Dong J3, Li Q6, Wang S3, Zhang Y6, Li H1, Gong T2, Shi Y2, Ni X1, Li J2, Zhou J2, Fan J7, Wu J1, Zhou X1, Hu M1, Wan J4, Yang W6, Li D3, Wu G3, Feng Z6, Gao GF6, Wang Y6, Jin Q5, Liu M1, Shu Y8.Author information 1Nanchang City Disease Control and Prevention, Nanchang, China.2Jiangxi Provincial Disease Control and Prevention, Nanchang, China.3National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Key Laboratory for Medical Virology, National Health and Family Planning Commission, Beijing, China.4The First Hospital of Nanchang, Nanchang, China.5MOH Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.6Chinese Center for Disease Control and Prevention, Beijing, China.7Donghu District Center for Disease Control and Prevention, Nanchang, China.8National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Key Laboratory for Medical Virology, National Health and Family Planning Commission, Beijing, China; Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Hangzhou, China. Electronic address: yshu@cnic.org.cn.AbstractBACKGROUND: Human infections with different avian influenza viruses--eg, H5N1, H9N2, and H7N9--have raised concerns about pandemic potential worldwide. We report the first human infection with a novel reassortant avian influenza A H10N8 virus.
Lancet.Lancet.2014 Feb 22;383(9918):714-21. doi: 10.1016/S0140-6736(14)60111-2. Epub 2014 Feb 5.
BACKGROUND: Human infections with different avian influenza viruses--eg, H5N1, H9N2, and H7N9--have raised concerns about pandemic potential worldwide. We report the first human infection with a novel reassortant avian influenza A H10N8 virus.METHODS: We obtained and analysed clinical, epidemiologic
PMID 24507376

Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system.

Akey DL1, Brown WC, Dutta S, Konwerski J, Jose J, Jurkiw TJ, DelProposto J, Ogata CM, Skiniotis G, Kuhn RJ, Smith JL.Author information 1Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.AbstractFlaviviruses, the human pathogens responsible for dengue fever, West Nile fever, tick-borne encephalitis, and yellow fever, are endemic in tropical and temperate parts of the world. The flavivirus nonstructural protein 1 (NS1) functions in genome replication as an intracellular dimer and in immune system evasion as a secreted hexamer. We report crystal structures for full-length, glycosylated NS1 from West Nile and dengue viruses. The NS1 hexamer in crystal structures is similar to a solution hexamer visualized by single-particle electron microscopy. Recombinant NS1 binds to lipid bilayers and remodels large liposomes into lipoprotein nanoparticles. The NS1 structures reveal distinct domains for membrane association of the dimer and interactions with the immune system and are a basis for elucidating the molecular mechanism of NS1 function.
Science (New York, N.Y.).Science.2014 Feb 21;343(6173):881-5. doi: 10.1126/science.1247749. Epub 2014 Feb 6.
Flaviviruses, the human pathogens responsible for dengue fever, West Nile fever, tick-borne encephalitis, and yellow fever, are endemic in tropical and temperate parts of the world. The flavivirus nonstructural protein 1 (NS1) functions in genome replication as an intracellular dimer and in immune s
PMID 24505133

Japanese Journal

Erythromycin-susceptible but clindamycin-resistant phenotype of ermB-PCR-positive clinical group B streptococci having IS1216E-inserted ermB

Moroi Hiroaki,Arakawa Yoshichika,Kimura Kouji,Ido Ayaka,Banno Hirotsugu,Jin Wanchun,Wachino Jun-ichi,Yamada Keiko,Kikkawa Fumitaka,Park Yeon-Joon
Japanese Journal of Infectious Diseases, 2019
… (lincosamide nucleotidyltransferase) genes were positive in all three clinical isolates. …
NAID 130007668501

Identification and characterization of UDP-glucose pyrophosphorylase in cyanobacteria Anabaena sp. PCC 7120

Kawano Yusuke,Sekine Midori,Ihara Masaki
Journal of bioscience and bioengineering 117(5), 531-538, 2014-05
Exopolysaccharides produced by photosynthetic cyanobacteria have received considerable attention in recent years for their potential applications in the production of renewable biofuels. Particularly, …
NAID 110009823126

In vivo glycorandomization による多様なグリコシド化合物の簡便な調製

戸谷希一郎
Trends in glycoscience and glycotechnology 23(129), 153-154, 2011-05-31
NAID 10029583040

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