Nicholas Noinaj

Nicholas Noinaj Profile Picture

Associate Professor
PhD, Biochemistry, University of Kentucky

Contact Info:
HOCK 333
Noinaj Laboratory

Training Group(s):
Biomolecular Structure and Biophysics
Microbiology, Immunology and Infectious Diseases
Membrane Biology

Active Mentor - currently hosting PULSe students for laboratory rotations and recruiting PULSe students into the laboratory; serves on preliminary exam committees

Current Research Interests:

My research interests are in understanding how pathogenic Gram-negative bacteria are able to use virulence factors found on their surface to mediate infection. These virulence factors are found in the outer membrane and belong to a class of surface proteins commonly referred to as outer membrane proteins (OMPs). In particular, my lab will investigate the multi-component complex called the BAM complex, which is responsible for the biogenesis of all OMPs, in hopes of understanding how it is able to fold and insert OMPs into the outer membrane. We will use a combination of techniques to accomplish this including X-ray crystallography, electron microscopy, crosslinking, and various functional assays. Our ultimate goal is to use the information from the structural and functional characterization as a starting point for drug discovery and development targeting the BAM complex in a species specific manner.

Selected Publications:

Imai Y, Meyer KJ, Iinishi A, Favre-Godal Q, Green R, Manuse S, Caboni M, Mori M, Niles S, Ghiglieri M, Honrao C, Ma X, Guo JJ, Makriyannis A, Linares-Otoya L, Böhringer N, Wuisan ZG, Kaur H, Wu R, Mateus A, Typas A, Savitski MM, Espinoza JL, O'Rourke A, Nelson KE, Hiller S, Noinaj N, Schäberle TF, D'Onofrio A, Lewis K. A new antibiotic selectively kills Gram-negative pathogens. Nature. 2019 Dec;576(7787):459-464.

Yadav R, Noinaj N, Ostan N, Moraes T, Stoudenmire J, Maurakis S, Cornelissen CN. Structural Basis for Evasion of Nutritional Immunity by the Pathogenic Neisseriae. Front Microbiol. 2020 Jan 10;10:2981.

Wu, R., Stephenson, R., Gichaba, A., & Noinaj, N. (2019). The big BAM theory: An open and closed case? Biochimica et Biophysica Acta (BBA) - Biomembranes, 183062. ​

Chen D, Dong G, Noinaj N, Huang R. (2019) Discovery of Bisubstrate Inhibitors for Protein N-Terminal Methyltransferase 1. J Med Chem, 62(7):3773-3779.

Noinaj N and Buchanan SK (Eds.) (2018) Current Opinion in Structural Biology - Membranes, 51:vii-viii. ​

Lundquist K, Bakelar J, Noinaj N, Gumbart JC. (2018) C-terminal kink formation is required for lateral gating in BamA. PNAS, 115(34):E7942-E7949 .

Sikora AE, Wierzbicki IH, Zielke RA, Ryner RF, Korotkov KV, Buchanan SK, and Noinaj N. (2018) Structural and functional insights into the role of BamD and BamE within the b-barrel assembly machinery in Neisseria gonorrhoeae. JBC, 293(4):1106-1119.

O’ Neil P, Richardson LGL, Paila YD, Piszczek G, Chakravarthy S, Noinaj N*, Schnell DJ*. The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts. PNAS. 2017, (in press).

Noinaj N, Gumbart JC, Buchanan SK. The β-barrel assembly machinery in motion. Nat Rev Microbiol 2017, 15(4):197-204.

Bakelar J, Buchanan SK, Noinaj N. Structural snapshots of the β-barrel assembly machinery. FEBS J 2016, doi: 10.1111/febs.13960.

Celia H, Noinaj N*, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R*, Buchanan SK*. Structural insight into the role of the Ton complex in energy transduction. Nature 2016, 538(7623):60-65.

Bakelar J, Buchanan SK, Noinaj N. The structure of the β-barrel assembly machinery complex. Science 2016, 351(6269):180-6.

O'Neil PK, Rollauer SE, Noinaj N, Buchanan SK. Fitting the pieces of the β-barrel assembly machinery complex. Biochemistry 2015, 54(41):6303-11.

Noinaj N, Kuszak AJ, Balusek C, Gumbart JC, Buchanan SK. Lateral opening and exit pore formation are required for BamA function. Structure 2014, 22(7):1055-62.

Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, Buchanan SK. Structural insight into the biogenesis of β-barrel membrane proteins. Nature 2013, 501(7467):385-90.

Noinaj N, Cornelissen CN, Buchanan SK. Structural insight into the lactoferrin receptors from pathogenic Neisseria. J. Structural Biology 2013, 184(1):83-92.

White JF, Noinaj N, Shibata Y, Love J, Kloss B, Xu F, Gvozdenovic-Jeremic J, Shah P, Shiloach J, Tate CG, Grisshammer R. Structure of the agonist-bound neurotensin receptor. Nature 2012, 490(7421):508-13.

Noinaj N, Buchanan SK, Cornelissen CN. The transferrin-iron import system from pathogenic Neisseria species. Mol Microbiol. 2012, 86(2):246-57.

Noinaj N, Easley NC, Oke M, Mizuno N, Gumbart J, Boura E, Steere AN, Zak O, Aisen P, Tajkhorshid E, Evans RW, Gorringe AR, Mason AB, Steven AC, Buchanan SK. Structural basis for iron piracy by pathogenic Neisseria. Nature 2012, 483(7387):53-8.

Noinaj N, Bosserman MA, Schickli MA, Piszczek G, Kharel MK, Pahari P, Buchanan SK, Rohr J. The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis. J Biol Chem. 2011 286(26):23533-43.

Noinaj N, Fairman JW, Buchanan SK. The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex. J Mol Biol. 2011 Mar 25;407(2):248-60.

Noinaj N, Guillier M, Barnard TJ, Buchanan SK. TonB-dependent transporters: regulation, structure, and function. Annu Rev Microbiol. 2010, 64:43-60.

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