Evidence map›Paper›PMID 16285741›Full record

ArticleBiochemistry2005

The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo.

Deborah L Perlstein, Jie Ge, Allison D Ortigosa, John H Robblee, Zhen Zhang, Mingxia Huang, JoAnne Stubbe

Abstract read
In one paragraph

Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Discovery of posttranslational maturation by self-subunit swapping.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  20. Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

7 authors.

Deborah L PerlsteinDepartments of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Jie Ge
Allison D Ortigosa
John H Robblee
Zhen Zhang
Mingxia Huang
JoAnne Stubbe

Funding

Ribonucleotide Reductase: Structure and FunctionR01GM029595 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI STUBBE, JOANNE · 1985 to 2016
$6.9M
CARCINOGENESIS AND DRUG DEVELOPMENTT32CA009112 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J · 1985 to 2005
$2.2M
Function and Regulation of DNA Damage Response GenesR01CA095207 · NCI · UNIVERSITY OF COLORADO DENVER · PI HUANG, MINGXIA · 2003 to 2007
$1.3M
MECHANISM OF DINUCLEAR FE-Y. FORMATION OF NDP REDUCTASER37GM029595 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 1988 to 1997
–
NCI NIH HHS 5T32 CA 09112-28NCI NIH HHS CA095207NCI NIH HHS R01 CA095207NCI NIH HHS T32 CA009112NIGMS NIH HHS GM29595NIGMS NIH HHS R01 GM029595
6 · The paper itself

Abstract

The class I ribonucleotide reductases (RNRs) are composed of two homodimeric subunits: R1 and R2. R2 houses a diferric-tyrosyl radical (Y*) cofactor. Saccharomyces cerevisiae has two R2s: Y2 (beta2) and Y4 (beta'2). Y4 is an unusual R2 because three residues required for iron binding have been mutated. While the heterodimer (betabeta') is thought to be the active form, several rnr4delta strains are viable. To resolve this paradox, N-terminally epitope-tagged beta and beta' were expressed in E. coli or integrated into the yeast genome. In vitro exchange studies reveal that when apo-(His6)-beta2 ((His)beta2) is mixed with beta'2, apo-(His)betabeta' forms quantitatively within 2 min. In contrast, holo-betabeta' fails to exchange with apo-(His)beta2 to form holo-(His)betabeta and beta'2. Isolation of genomically encoded tagged beta or beta' from yeast extracts gave a 1:1 complex of beta and beta', suggesting that betabeta' is the active form. The catalytic activity, protein concentrations, and Y* content of the rnr4delta and wild type (wt) strains were compared to clarify the role of beta' in vivo. The Y* content of rnr4delta is 15-fold less than that of wt, consistent with the observed low activity of rnr4delta extracts (<0.01 nmol min(-1) mg(-1)) versus wt (0.06 +/- 0.01 nmol min(-1) mg(-1)). (FLAG)beta2 isolated from the rnr4delta strain has a specific activity of 2 nmol min(-1) mg(-1), similar to that of reconstituted apo-(His)beta2 (10 nmol min(-1) mg(-1)), but significantly less than holo-(His)betabeta' (approximately 2000 nmol min(-1) mg(-1)). These studies together demonstrate that beta' plays a crucial role in cluster assembly in vitro and in vivo and that the active form of the yeast R2 is betabeta'.

Indexed as

Amino Acid SequenceApoenzymesCalorimetry, Differential ScanningChromatography, AffinityCircular DichroismElectron Spin Resonance SpectroscopyElectrophoresis, Polyacrylamide GelHistidineMolecular Sequence DataProtein Structure, QuaternaryProtein SubunitsRibonucleotide ReductasesSaccharomyces cerevisiaeApoenzymesHistidineProtein Subunitsribonucleotide reductase R2 subunitRibonucleotide Reductases

Identifiers

PMID16285741
PMCPMC4669231

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.