Evidence map›Paper›PMID 9358180›Full record

ArticleNucleic acids research1997

Baculovirus-mediated expression and characterization of the full-length murine DNA methyltransferase.

S Pradhan, D Talbot, M Sha, J Benner, L Hornstra, E Li, R Jaenisch, R J Roberts

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. Article
  3. Dnmt1 has de novo activity targeted to transposable elements.Nature structural & molecular biology · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Global delay in nascent strand DNA methylation.Nature structural & molecular biology · 2018
    Article
  8. Article
  9. Crystal Structure of Human DNA Methyltransferase 1.Journal of molecular biology · 2015
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. MicroRNA-29 family reverts aberrant methylation in lung cancer by targeting DNA methyltransferases 3A and 3B.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

S PradhanNew England Biolabs, 32 Tozer Road, Beverly, MA 01915, USA.
D Talbot
M Sha
J Benner
L Hornstra
E Li
R Jaenisch
R J Roberts
New England Biolabs (United States) · US

Funding

DNA METHYLATION IN GENOMIC IMPRINTING AND DEVELOPMENTR01GM052106 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI LI, EN · 1995 to 2004
$1.3M
RETROVIRUSES, ONCOGENES &MAMMALIAN DEVELOPMENTR35CA044339 · NCI · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI JAENISCH, RUDOLF · 1987 to 2000
$981k
STUDIES OF M5-CYTOSINE METHYLASESR01GM046127 · NIGMS · NEW ENGLAND BIOLABS, INC. · PI ROBERTS, RICHARD J. · 1991 to 1998
–
NCI NIH HHS CA44339NIGMS NIH HHS GM46127NIGMS NIH HHS GM52106
6 · The paper itself

Abstract

The original cDNA sequence reported for the murine DNA methyltransferase (MTase) was not full length. Recently, additional cDNA sequences have been reported that lie upstream of the original and contain an extended open reading frame with three additional ATGs in frame with the coding region [Tucker et al . (1996) Proc. Natl. Acad. Sci. USA , 93, 12920-12925; Yoder et al . (1996) J. Biol. Chem . 271, 31092-31097]. Genomic DNA upstream of this ATG contains two more ATGs in frame and no obvious splice site. We have constructed, and expressed in baculovirus, MTase clones that begin at each of these four ATGs and examined their properties. Constructs beginning with any of the first three ATGs as their initiator methionines give a predominant DNA MTase band of approximately 185 kDa on SDS-PAGE corresponding to translational initiation at the third ATG. The fourth ATG construct gives a much smaller protein band of 173 kDa. The 185 kDa protein was purified by HPLC, characterized by mass spectrometry and has a measured molecular mass of 184 +/- 0.5 kDa. All of these MTases were functional in vitro and steady state kinetic analysis showed that the recombinant proteins exhibit similar kinetic properties irrespective of their length. The homogeneous recombinant enzyme from the fourth ATG construct shows a 2.5-fold preference for a hemi-methylated DNA substrate as compared to an unmethylated substrate, whereas the 185 kDa protein is equally active on both substrates. The kinetic properties of the recombinant enzyme are similar to those reported for the native MTase derived from murine erythroleukemia cells. The new clones are capable of yielding large quantities of intact MTases for further structural and functional studies.

Indexed as

Amino Acid SequenceAnimalsBaculoviridaeCell LineCloning, MolecularDNA Modification MethylasesDNA, Single-StrandedGene ExpressionGenetic VectorsMiceMolecular Sequence DataMolecular WeightOligonucleotidesProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSpodopteraDNA Modification MethylasesDNA, Single-StrandedOligonucleotidesRecombinant Fusion Proteins

Identifiers

PMID9358180
PMCPMC147102
OpenAlexW1997056426

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.