Evidence map›Paper›PMID 20439755›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Direct role for the RNA polymerase domain of T7 primase in primer delivery.

Bin Zhu, Seung-Joo Lee, Charles C Richardson

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Computationally exploring the mechanism of bacteriophage T7 gp4 helicase translocating along ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Bacteriophage T7 DNA polymerase - sequenase.Frontiers in microbiology · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. Molecular interactions in the priming complex of bacteriophage T7.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Choreography of bacteriophage T7 DNA replication.Current opinion in chemical biology · 2011
    Review
  15. Bypass of a nick by the replisome of bacteriophage T7.The Journal of biological chemistry · 2011
    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

3 authors at 1 institution in 1 country.

Bin ZhuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Seung-Joo Lee
Charles C Richardson
Harvard University · US

Funding

STRUCTURE AND SYNTHESIS OF DNAR01GM054397 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RICHARDSON, CHARLES C. · 1996 to 2011
$7.6M
NIGMS NIH HHS GM 54397NIGMS NIH HHS R01 GM054397
6 · The paper itself

Abstract

Gene 4 protein (gp4) encoded by bacteriophage T7 contains a C-terminal helicase and an N-terminal primase domain. After synthesis of tetraribonucleotides, gp4 must transfer them to the polymerase for use as primers to initiate DNA synthesis. In vivo gp4 exists in two molecular weight forms, a 56-kDa form and the full-length 63-kDa form. The 56-kDa gp4 lacks the N-terminal Cys(4) zinc-binding motif important in the recognition of primase sites in DNA. The 56-kDa gp4 is defective in primer synthesis but delivers a wider range of primers to initiate DNA synthesis compared to the 63-kDa gp4. Suppressors exist that enable the 56-kDa gp4 to support the growth of T7 phage lacking gene 4 (T7Delta4). We have identified 56-kDa DNA primases defective in primer delivery by screening for their ability to support growth of T7Delta4 phage in the presence of this suppressor. Trp69 is critical for primer delivery. Replacement of Trp69 with lysine in either the 56- or 63-kDa gp4 results in defective primer delivery with other functions unaffected. DNA primase harboring lysine at position 69 fails to stabilize the primer on DNA. Thus, a primase subdomain not directly involved in primer synthesis is involved in primer delivery. The stabilization of the primer by DNA primase is necessary for DNA polymerase to initiate synthesis.

Indexed as

Models, MolecularBacteriophage T7DNA-Directed RNA PolymerasesDNA PrimaseDNA PrimersDNA ReplicationProtein Structure, TertiaryTryptophanViral Proteinsbacteriophage T7 RNA polymeraseDNA-Directed RNA PolymerasesDNA PrimaseDNA PrimersTryptophanViral Proteins

Identifiers

PMID20439755
PMCPMC2889121
OpenAlexW1976786777

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.