Evidence map›Paper›PMID 17644595›Full record

ArticleJournal of bacteriology2007

Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum.

David M Wolfe, Yaoping Zhang, Gary P Roberts

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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  9. P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.Proceedings of the National Academy of Sciences of the United States of America · 2013
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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.

David M WolfeDepartment of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA.
Yaoping Zhang
Gary P Roberts
University of Wisconsin–Madison · US

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
PII: multiple homologs of a global regulatorR01GM065891 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERTS, GARY PAUL · 2002 to 2011
$2.0M
Molecular basis of PII functionR56GM065891 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERTS, GARY PAUL · 2007 to 2007
$203k
NIGMS NIH HHS GM65891NIGMS NIH HHS R01 GM065891NIGMS NIH HHS R56 GM065891NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

The nitrogen regulatory protein P(II) and the ammonia gas channel AmtB are both found in most prokaryotes. Interaction between these two proteins has been observed in several organisms and may regulate the activities of both proteins. The regulation of their interaction is only partially understood, and we show that in Rhodospirillum rubrum one P(II) homolog, GlnJ, has higher affinity for an AmtB(1)-containing membrane than the other two P(II) homologs, GlnB and GlnK. This interaction strongly favors the nonuridylylated form of GlnJ and is disrupted by high levels of 2-ketoglutarate (2-KG) in the absence of ATP or low levels of 2-KG in the presence of ATP. ADP inhibits the destabilization of the GlnJ-AmtB(1) complex in the presence of ATP and 2-KG, supporting a role for P(II) as an energy sensor measuring the ratio of ATP to ADP. In the presence of saturating levels of ATP, the estimated K(d) of 2-KG for GlnJ bound to AmtB(1) is 340 microM, which is higher than that required for uridylylation of GlnJ in vitro, about 5 microM. This supports a model where multiple 2-KG and ATP molecules must bind a P(II) trimer to stimulate release of P(II) from AmtB(1), in contrast to the lower 2-KG requirement for productive uridylylation of P(II) by GlnD.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBacterial ProteinsBlotting, WesternCation Transport ProteinsKetoglutaric AcidsPII Nitrogen Regulatory ProteinsProtein BindingQuaternary Ammonium CompoundsRhodospirillum rubrumAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsCation Transport ProteinsKetoglutaric AcidsPIID regulatory protein, BacteriaPII Nitrogen Regulatory ProteinsQuaternary Ammonium Compounds

Identifiers

PMID17644595
PMCPMC2045211
OpenAlexW2074953002

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.