Evidence map›Paper›PMID 10542161›Full record

ArticleJournal of bacteriology1999

Characterization of a Hank's type serine/threonine kinase and serine/threonine phosphoprotein phosphatase in Pseudomonas aeruginosa.

S Mukhopadhyay, V Kapatral, W Xu, A M Chakrabarty

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 54 citations in OpenAlex.

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  6. Mutation in theGenes · 2018
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  18. A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
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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

4 authors at 2 institutions in 1 country.

S MukhopadhyayDepartment of Microbiology and Immunology, University of Illinois College of Medicine, Chicago, Illinois 60612, USA.
V Kapatral
W Xu
A M Chakrabarty
University of Illinois Chicago · USUniversity of Illinois Urbana-Champaign · US

Funding

PSEUDOMONAS INFECTION IN CYSTIC FIBROSISR01AI016790 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHAKRABARTY, ANANDA MOHAN · 1985 to 2000
$250k
PSEUDOMONAS INFECTION IN CYSTIC FIBROSISR37AI016790 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHAKRABARTY, ANANDA MOHAN · 1986 to 1995
–
NIAID NIH HHS AI 16790-18
6 · The paper itself

Abstract

Pseudomonas aeruginosa is an opportunistic pathogen that causes infections in eye, urinary tract, burn, and immunocompromised patients. We have cloned and characterized a serine/threonine (Ser/Thr) kinase and its cognate phosphoprotein phosphatase. By using oligonucleotides from the conserved regions of Ser/Thr kinases of mycobacteria, an 800-bp probe was used to screen P. aeruginosa PAO1 genomic library. A 20-kb cosmid clone was isolated, from which a 4.5-kb DNA with two open reading frames (ORFs) were subcloned. ORF1 was shown to encode Ser/Thr phosphatase (Stp1), which belongs to the PP2C family of phosphatases. Overlapping with the stp1 ORF, an ORF encoding Hank's type Ser/Thr kinase was identified. Both ORFs were cloned in pGEX-4T1 and expressed in Escherichia coli. The overexpressed proteins were purified by glutathione-Sepharose 4B affinity chromatography and were biochemically characterized. The Stk1 kinase is 39 kDa and undergoes autophosphorylation and can phosphorylate eukaryotic histone H1. A site-directed Stk1 (K86A) mutant was shown to be incapable of autophosphorylation. A two-dimensional phosphoamino acid analysis of Stk1 revealed strong phosphorylation at a threonine residue and weak phosphorylation at a serine residue. The Stp1 phosphatase is 27 kDa and is an Mn(2+)-, but not a Ca(2+)- or a Mg(2+)-, dependent Ser/Thr phosphatase. Its activity is inhibited by EDTA and NaF, but not by okadaic acid, and is similar to that of PP2C phosphatase.

Indexed as

Genes, BacterialAmino Acid SequenceCloning, MolecularMolecular Sequence DataMultigene FamilyPhosphoamino AcidsPhosphoprotein PhosphatasesPhosphorylationPrecipitin TestsProtein Serine-Threonine KinasesPseudomonas aeruginosaRecombinant Fusion ProteinsReverse Transcriptase Polymerase Chain ReactionSequence AlignmentSerineThreoninePhosphoamino AcidsPhosphoprotein PhosphatasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSerineThreonine

Identifiers

PMID10542161
PMCPMC94124
OpenAlexW2157532899

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.