{"refrec":{"BRefID":261749,"RR":"<b>Georlette, D.; Jonsson, Z.O.; Van Petegem, F.; Chessa, J.P.; Van Beeumen, J.; Hübscher, U.; Gerday, C.</b> (2000). A DNA ligase from the psychrophile <i>Pseudoalteromonas haloplanktis</i> gives insights into the adaptation of proteins to low temperatures. <i>Eur. J. Biochem. 267(12)</i>: 3502-3512. <a href=\"http://dx.doi.org/10.1046/j.1432-1327.2000.01377.x\" target=\"_blank\">dx.doi.org/10.1046/j.1432-1327.2000.01377.x</a>","BEntID":253767,"PublicFlag":1,"CheckedFlag":1,"wosflag":null,"vabbflag":null,"RefStringPartII":". <i>Eur. J. Biochem. 267(12)</i>: 3502-3512. <a href=\"https://dx.doi.org/10.1046/j.1432-1327.2000.01377.x\" target=\"_blank\">https://dx.doi.org/10.1046/j.1432-1327.2000.01377.x</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Georlette, D.; Jonsson, Z.O.; Van Petegem, F.; Chessa, J.P.; Van Beeumen, J.; Hübscher, U.; Gerday, C.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Georlette, D. <i>et al.</i>","Englishabstract":"The cloning, overexpression and characterization of a cold-adapted DNA ligase from the Antarctic sea water bacterium <i>Pseudoalteromonas haloplanktis</i> are described. Protein sequence analysis revealed that the cold-adapted <i>Ph</i> DNA ligase shows a significant level of sequence similarity to other NAD<sup>+</sup>-dependent DNA ligases and contains several previously described sequence motifs. Also, a decreased level of arginine and proline residues in <i>Ph</i> DNA ligase could be involved in the cold-adaptation strategy. Moreover, 3D modelling of the N-terminal domain of <i>Ph</i> DNA ligase clearly indicates that this domain is destabilized compared with its thermophilic homologue. The recombinant <i>Ph</i> DNA ligase was overexpressed in <i>Escherichia coli</i> and purified to homogeneity. Mass spectroscopy experiments indicated that the purified enzyme is mainly in an adenylated form with a molecular mass of 74&nbsp;593&nbsp;Da. <i>Ph</i> DNA ligase shows similar overall catalytic properties to other NAD<sup>+</sup>-dependent DNA ligases but is a cold-adapted enzyme as its catalytic efficiency (<i>k</i><sub>cat</sub>/<i>K</i><sub>m</sub>) at low and moderate temperatures is higher than that of its mesophilic counterpart <i>E.&nbsp;coli</i> DNA ligase. A kinetic comparison of three enzymes adapted to different temperatures (<i>P.&nbsp;haloplanktis</i>,<i> E.&nbsp;coli </i>and<i> Thermus scotoductus</i> DNA ligases) indicated that an increased <i>k</i><sub>cat</sub> is the most important adaptive parameter for enzymatic activity at low temperatures, whereas a decreased <i>K</i><sub>m</sub> for the nicked DNA substrate seems to allow <i>T.&nbsp;scotoductus</i> DNA ligase to work efficiently at high temperatures. Besides being useful for investigation of the adaptation of enzymes to extreme temperatures, <i>P.&nbsp;haloplanktis</i> DNA ligase, which is very efficient at low temperatures, offers a novel tool for biotechnology.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"A DNA ligase from the psychrophile <i>Pseudoalteromonas haloplanktis</i> gives insights into the adaptation of proteins to low temperatures","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:32:52.928458","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"NAD(+)-dependent DNA ligase; psychrophile; thermophile; structuralcomparison; overexpression","OtherDescriptors":null,"Notes":null,"AnaPub":2000,"MonPub":null,"DateUpdate":"2016-10-10","DateCreate":"2016-10-03","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000087624600013","VABBcode":null,"OpenAcc":1,"DOI":"10.1046/j.1432-1327.2000.01377.x"},"refs":null,"anarec":{"AnaID":261749,"PubliDate":2000,"Pagination":"3502-3512","XtraPublOfAnaID":null,"ISBN":null,"Volume":"267","Issue":"12","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42671,"SerRR":"European Journal of Biochemistry. 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