Author

A. Turdiev

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Organism:E. coli· 1 Assay:proteomics· 1

Frequent Co-Authors

H. Turdiev· 3 shared V. T. Lee· 3 shared B. W. Anderson· 2 shared J. D. Wang· 2 shared J. Yang· 2 shared C. A. Weiss· 1 shared D. Amador-Noguez· 1 shared D. M. Stevenson· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersMicrobiology

H. Turdiev

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3 papers

Recent·Most cited

The nucleotide messenger (p)ppGpp is a co-repressor of the purine synthesis transcription regulator PurR in Firmicutes

B. W. Anderson, M. A. Schumacher, J. Yang, A. Turdiev, H. Turdiev, Q. He, V. T. Lee, R. G. Brennan, J. D. Wang

This study shows (p)ppGpp acts as a co-repressor of PurR in Firmicutes, downregulating purine synthesis by enhancing PurR DNA binding, with implications across environments from the gut to pathogens.

bioRxiv · Dec 2, 2020 · PreprintMicrobiology

Systemic characterization of pppGpp, ppGpp and pGpp targets in Bacillus reveal NahA converts (p)ppGpp to pGpp to regulate alarmone composition and signaling

J. Yang, B. W. Anderson, A. Turdiev, H. Turdiev, D. M. Stevenson, D. Amador-Noguez, V. T. Lee, J. D. Wang

The paper identifies pGpp as a third alarmone in Bacillus and shows NahA converts (p)ppGpp to pGpp, altering alarmone composition and stress response.

bioRxiv · Mar 23, 2020 · PreprintMicrobiology

Oligoribonuclease functions as a diribonucleotidase to bypass a key bottleneck in RNA degradation

S.-K. Kim, J. D. Lormand, C. A. Weiss, K. A. Eger, H. Turdiev, A. Turdiev, W. C. Winkler, H. Sondermann, V. T. Lee

This study identifies oligoribonuclease (Orn) as a dedicated diribonucleotidase essential for completing RNA degradation by clearing diribonucleotides, which otherwise impact cellular viability.

bioRxiv · Feb 11, 2019 · PreprintMicrobiology