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Deoxyribonucleoside kinases in two aquatic bacteria with high specificity for thymidine and deoxyadenosine.

Tinta, Tinkara LU ; Slot Christiansen, Louise LU ; Konrad, Anke; Liberles, David A; Turk, Valentina; Munch-Petersen, Birgitte; Piskur, Jure LU and Clausen, Anders Ranegaard LU (2012) In FEMS Microbiology Letters 331(2). p.120-127
Abstract
Deoxyribonucleoside kinases (dNKs) are essential in the mammalian cell but their 'importance' in bacteria, especially aquatic ones, is less clear. We studied two aquatic bacteria, Gram-negative Flavobacterium psychrophilum JIP02/86 and Polaribacter sp. MED152, for their ability to salvage deoxyribonucleosides (dNs). Both had a Gram-positive-type thymidine kinase (TK1), which could phosphorylate thymidine, and one non-TK1 dNK, which could efficiently phosphorylate deoxyadenosine and slightly also deoxycytosine. Surprisingly, the four tested dNKs could not phosphorylate deoxyguanosine, and apparently, these two bacteria are missing this activity. When tens of available aquatic bacteria genomes were examined for the presence of dNKs, a... (More)
Deoxyribonucleoside kinases (dNKs) are essential in the mammalian cell but their 'importance' in bacteria, especially aquatic ones, is less clear. We studied two aquatic bacteria, Gram-negative Flavobacterium psychrophilum JIP02/86 and Polaribacter sp. MED152, for their ability to salvage deoxyribonucleosides (dNs). Both had a Gram-positive-type thymidine kinase (TK1), which could phosphorylate thymidine, and one non-TK1 dNK, which could efficiently phosphorylate deoxyadenosine and slightly also deoxycytosine. Surprisingly, the four tested dNKs could not phosphorylate deoxyguanosine, and apparently, these two bacteria are missing this activity. When tens of available aquatic bacteria genomes were examined for the presence of dNKs, a majority had at least a TK1-like gene, but several lacked any dNKs. Apparently, among aquatic bacteria, the role of the dN salvage varies. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
aquatic bacteria, 3H-thymidine incorporation, deoxyribonucleoside kinase, nucleoside salvage
in
FEMS Microbiology Letters
volume
331
issue
2
pages
120 - 127
publisher
Elsevier
external identifiers
  • wos:000304187800005
  • pmid:22462611
  • scopus:84861233766
ISSN
1574-6968
DOI
10.1111/j.1574-6968.2012.02565.x
language
English
LU publication?
yes
id
86655bac-31d1-4d5e-a544-af86fecfbf1f (old id 2520042)
date added to LUP
2012-05-08 11:49:15
date last changed
2017-01-01 03:01:42
@article{86655bac-31d1-4d5e-a544-af86fecfbf1f,
  abstract     = {Deoxyribonucleoside kinases (dNKs) are essential in the mammalian cell but their 'importance' in bacteria, especially aquatic ones, is less clear. We studied two aquatic bacteria, Gram-negative Flavobacterium psychrophilum JIP02/86 and Polaribacter sp. MED152, for their ability to salvage deoxyribonucleosides (dNs). Both had a Gram-positive-type thymidine kinase (TK1), which could phosphorylate thymidine, and one non-TK1 dNK, which could efficiently phosphorylate deoxyadenosine and slightly also deoxycytosine. Surprisingly, the four tested dNKs could not phosphorylate deoxyguanosine, and apparently, these two bacteria are missing this activity. When tens of available aquatic bacteria genomes were examined for the presence of dNKs, a majority had at least a TK1-like gene, but several lacked any dNKs. Apparently, among aquatic bacteria, the role of the dN salvage varies.},
  author       = {Tinta, Tinkara and Slot Christiansen, Louise and Konrad, Anke and Liberles, David A and Turk, Valentina and Munch-Petersen, Birgitte and Piskur, Jure and Clausen, Anders Ranegaard},
  issn         = {1574-6968},
  keyword      = {aquatic bacteria,3H-thymidine incorporation,deoxyribonucleoside kinase,nucleoside salvage},
  language     = {eng},
  number       = {2},
  pages        = {120--127},
  publisher    = {Elsevier},
  series       = {FEMS Microbiology Letters},
  title        = {Deoxyribonucleoside kinases in two aquatic bacteria with high specificity for thymidine and deoxyadenosine.},
  url          = {http://dx.doi.org/10.1111/j.1574-6968.2012.02565.x},
  volume       = {331},
  year         = {2012},
}