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Article: A novel putative transcription factor protein MYT2 that preferentially binds supercoiled DNA and induces DNA synthesis in quiescent cells

TitleA novel putative transcription factor protein MYT2 that preferentially binds supercoiled DNA and induces DNA synthesis in quiescent cells
Authors
Issue Date2000
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
FEBS Letters, 2000, v. 473, p. 363-369 How to Cite?
AbstractMyelin transcription factor 2 (MYT2), a putative transcription factor found in the human central nervous system, was cloned from an expression cDNA library from human T-cells. MYT2 shares weak similarity to bacterial type I topoisomerases and shares 63% sequence identity to a replicase from Leuconostoc mesenteroides. MYT2 preferentially binds supercoiled DNA (scDNA). Incubation of MYT2 and scDNA at or above equal molar ratios generated topoisomer-like patterns that were abolished by deproteination. Thus, MYT2 appears to relax scDNA via a non-enzymatic mechanism. The banding pattern of MYT2–scDNA complexes was shown to be quantisized, saturable and sequence-independent. Microinjection of MYT2 mRNA induced Go growth-arrested NIH 3T3 cells to enter the S phase of the cell cycle.
Persistent Identifierhttp://hdl.handle.net/10722/224796
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026

 

DC FieldValueLanguage
dc.contributor.authorShao, W-
dc.contributor.authorLee, AY-
dc.contributor.authorGulnik, S-
dc.contributor.authorGustchina, E-
dc.contributor.authorLiu, YL-
dc.contributor.authorKung, HF-
dc.contributor.authorErickson, JW-
dc.date.accessioned2016-04-15T04:07:12Z-
dc.date.available2016-04-15T04:07:12Z-
dc.date.issued2000-
dc.identifier.citationFEBS Letters, 2000, v. 473, p. 363-369-
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/10722/224796-
dc.description.abstractMyelin transcription factor 2 (MYT2), a putative transcription factor found in the human central nervous system, was cloned from an expression cDNA library from human T-cells. MYT2 shares weak similarity to bacterial type I topoisomerases and shares 63% sequence identity to a replicase from Leuconostoc mesenteroides. MYT2 preferentially binds supercoiled DNA (scDNA). Incubation of MYT2 and scDNA at or above equal molar ratios generated topoisomer-like patterns that were abolished by deproteination. Thus, MYT2 appears to relax scDNA via a non-enzymatic mechanism. The banding pattern of MYT2–scDNA complexes was shown to be quantisized, saturable and sequence-independent. Microinjection of MYT2 mRNA induced Go growth-arrested NIH 3T3 cells to enter the S phase of the cell cycle.-
dc.languageeng-
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet-
dc.relation.ispartofFEBS Letters-
dc.rightsPosting accepted manuscript (postprint): © <year>. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.subject.meshDNA - biosynthesis - metabolism-
dc.subject.meshDNA Topoisomerases, Type I - metabolism-
dc.subject.meshDNA, Superhelical - metabolism - ultrastructure-
dc.subject.meshDNA-Binding Proteins - genetics - isolation & purification - metabolism-
dc.subject.meshTranscription Factors - genetics - isolation & purification - metabolism-
dc.titleA novel putative transcription factor protein MYT2 that preferentially binds supercoiled DNA and induces DNA synthesis in quiescent cells-
dc.typeArticle-
dc.identifier.emailKung, HF: hkung@hkucc.hku.hk-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/S0014-5793(00)01536-2-
dc.identifier.pmid10818241-
dc.identifier.scopuseid_2-s2.0-0034685694-
dc.identifier.hkuros51917-
dc.identifier.volume473-
dc.identifier.spage363-
dc.identifier.epage369-
dc.publisher.placeNetherlands-

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