Author

A. R. Reddi

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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Biochemistry· 3 Cell Biology· 3 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:cell type annotation· 5 Research Focus:cell signaling & trafficking· 4 Assay:proteomics· 4 Organism:human· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:host-pathogen & immune response· 2 Organism:C. elegans· 1

Frequent Co-Authors

I. Bohovych· 3 shared J. V. Dietz· 3 shared O. Khalimonchuk· 3 shared A. E. Medlock· 2 shared C. M. Moore· 2 shared H. A. Dailey· 2 shared L. D. Williams· 2 shared M. M. Willoughby· 2 shared

Activity by Year

2018-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersCell Biology

I. Bohovych

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Heme oxygenase-2 (HO-2) binds and buffers labile heme, which is largely oxidized, in human embryonic kidney cells

D. A. Hanna, C. M. Moore, L. Liu, X. Yuan, A. S. Fleischhacker, I. Hamza, S. W. Ragsdale, A. R. Reddi

This study shows HO-2 binds and buffers oxidized labile heme in HEK293 cells, regulating heme homeostasis by controlling bioavailability rather than degrading heme under non-stress conditions.

bioRxiv · Jun 6, 2021Cell Biology

Mitochondrial Contact Site and Cristae Organizing System (MICOS) Machinery Supports Heme Biosynthesis by Enabling Optimal Performance of Ferrochelatase

J. V. Dietz, M. M. Willoughby, R. B. Piel, T. A. Ross, I. Bohovych, H. G. Addis, J. L. Fox, W. N. Lanzilotta, H. A. Dailey, J. A. Wohlschlegel, A. R. Reddi, A. E. Medlock, O. Khalimonchuk

The paper investigates the role of MICOS in regulating ferrochelatase activity and heme biosynthesis in yeast, showing that MICOS disruption leads to toxic tetrapyrrole accumulation.

bioRxiv · Jun 1, 2021Biochemistry

The terminal heme synthetic enzyme, Coproheme Decarboxylase, coordinates heme synthesis and uptake in response to iron in Mycobacteria

R. K. Donegan, J. Copeland, S. Edgha, G. Brown, O. F. Hale, A. Mitra, H. Yang, H. A. Dailey, M. Niederweis, P. Jain, A. R. Reddi

This study identifies Coproheme Decarboxylase (ChdC) as a regulator of heme synthesis and uptake in Mycobacterium tuberculosis, showing it controls heme bioavailability and iron acquisition in response to iron availability.

bioRxiv · May 10, 2021 · PreprintMicrobiology

Using genetically encoded heme sensors to probe the mechanisms of heme uptake and homeostasis in Candida albicans

Z. Weissman, M. Pinsky, R. K. Donegan, A. R. Reddi, D. Kornitzer

This study uses genetically encoded heme sensors to show that C. albicans takes up heme from hemoglobin and hemin via different pathways and uses Hmx1 to prevent heme toxicity.

bioRxiv · Jul 26, 2020Microbiology

Human Ribosomal G-Quadruplexes Regulate Heme Bioavailability

S. Mestre-Fos, C. Ito, C. M. Moore, A. R. Reddi, L. D. Williams

This study shows human ribosomes form G-quadruplexes in vivo that regulate heme bioavailability through interactions with G4 ligands and heme sensors.

bioRxiv · Apr 15, 2020Biochemistry

The heme biosynthetic enzyme, 5-aminolevulinic acid synthase (ALAS), and GTPases in control of mitochondrial dynamics and ER contact sites, regulate heme mobilization to the nucleus.

O. Martinez-Guzman, M. M. Willoughby, A. Saini, J. V. Dietz, I. Bohovych, A. E. Medlock, O. Khalimonchuk, A. R. Reddi

The paper develops a live-cell assay to study heme trafficking and identifies ALAS and GTPases as regulators of heme mobilization from mitochondria to the nucleus.

bioRxiv · Aug 13, 2019 · PreprintCell Biology

Mitochondrial-nuclear heme trafficking is regulated by GTPases that control mitochondrial dynamics.

O. Martinez-Guzman, J. V. Dietz, I. Bohovych, A. W. Medlock, O. Khalimonchuk, A. R. Reddi

The paper investigates mitochondrial-nuclear heme trafficking and identifies GTPases regulating this process, showing heme moves faster to the nucleus than to the matrix or cytosol.

bioRxiv · Feb 4, 2019 · PreprintCell Biology

Multiple prebiotic metals mediate translation

M. S. Bray, T. K. Lenz, J. W. Haynes, J. C. Bowman, A. S. Petrov, A. R. Reddi, N. V. Hud, L. D. Williams, J. B. Glass

The paper tests whether Fe2+ and Mn2+ could replace Mg2+ in ribosome function under ancient Earth conditions, finding they can mediate translation and associate with the ribosome.

bioRxiv · Oct 4, 2018Biochemistry