tpr domain Search Results


tpr domains  (Schmid GmbH)
90
Schmid GmbH tpr domains
Tpr Domains, supplied by Schmid GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tpr domains  (InterPro Inc)
90
InterPro Inc tpr domains
PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain <t>(TPR</t> domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.
Tpr Domains, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tpr+domain/pmc06069109-124-0-14?v=InterPro+Inc
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tpr domains - by Bioz Stars, 2026-08
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conserved tpr domain  (InterPro Inc)
90
InterPro Inc conserved tpr domain
PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain <t>(TPR</t> domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.
Conserved Tpr Domain, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tpr+domain/pm40130841-128-48-53?v=InterPro+Inc
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conserved tpr domain - by Bioz Stars, 2026-08
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protein repeat domain tpr pd00126a  (Nuclea Biotechnologies)
90
Nuclea Biotechnologies protein repeat domain tpr pd00126a
PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain <t>(TPR</t> domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.
Protein Repeat Domain Tpr Pd00126a, supplied by Nuclea Biotechnologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tpr+domain/us06919193-1845-0-10?v=Nuclea+Biotechnologies
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protein repeat domain tpr pd00126a - by Bioz Stars, 2026-08
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n-terminal tpr domain of a human ser/thr protein phosphatase  (Federation of European Neuroscience Societies)
90
Federation of European Neuroscience Societies n-terminal tpr domain of a human ser/thr protein phosphatase
PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain <t>(TPR</t> domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.
N Terminal Tpr Domain Of A Human Ser/Thr Protein Phosphatase, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tpr+domain/pm11240121-2-18-40?v=Federation+of+European+Neuroscience+Societies
Average 90 stars, based on 1 article reviews
n-terminal tpr domain of a human ser/thr protein phosphatase - by Bioz Stars, 2026-08
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tetratrico-peptide repeat (tpr) domains  (Schmid GmbH)
90
Schmid GmbH tetratrico-peptide repeat (tpr) domains
PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain <t>(TPR</t> domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.
Tetratrico Peptide Repeat (Tpr) Domains, supplied by Schmid GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tpr+domain/10__3109_slash_1040841x__2014__947239-57-84-127?v=Schmid+GmbH
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tetratrico-peptide repeat (tpr) domains - by Bioz Stars, 2026-08
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codon-optimized dna sequence encoding the tpr domain of mouse klc1  (GenScript corporation)
90
GenScript corporation codon-optimized dna sequence encoding the tpr domain of mouse klc1
PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain <t>(TPR</t> domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.
Codon Optimized Dna Sequence Encoding The Tpr Domain Of Mouse Klc1, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tpr+domain/pm33838110-216-9-33?v=GenScript+corporation
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codon-optimized dna sequence encoding the tpr domain of mouse klc1 - by Bioz Stars, 2026-08
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Image Search Results


PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain (TPR domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.

Journal: mBio

Article Title: An Aspartate-Specific Solute-Binding Protein Regulates Protein Kinase G Activity To Control Glutamate Metabolism in Mycobacteria

doi: 10.1128/mBio.00931-18

Figure Lengend Snippet: PknG activation by glutamate was indirect, and PknG function required the conserved protein interaction domain (TPR domain). (A) Kinase activity of recombinant PknG toward GarA was independent of glutamate. Kinase reactions in the presence or absence of glutamate were sampled at the indicated times. Phosphorylation of GarA was detected by the known decrease in mobility of phospho-GarA in SDS-PAGE ( , ). The rate of GarA phosphorylation was similar to that seen in previous studies of PknG and was unchanged by the addition of glutamate. Images are representative of three independent experiments. Similar results were obtained with other putative activators: glutamine, aspartate, and α-ketoglutarate. (B) PknG homologues from Actinomycetales have a variable N-terminal domain, sometimes lack the Rdx domain (absent from homologues in the Corynebacteriaceae ), and always have a tetratricopeptide repeat (TPR) domain. (C) Truncated PknG lacking the Rdx was able to restore the ability of pknG -deficient M. smegmatis to grow on minimal medium containing glutamate as the sole nitrogen source, but truncated PknG lacking the TPR domain did not improve growth. Error bars show standard deviations from three wells, and the growth curve is representative of three independent experiments.

Article Snippet: TPR domains have been identified in kinases from multiple bacterial phyla (>1,000 listed in Interpro [ ]), suggesting that TPR-mediated protein interaction could be a widespread regulatory mechanism of bacterial serine/threonine protein kinases.

Techniques: Activation Assay, Activity Assay, Recombinant, Phospho-proteomics, SDS Page