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Bogdan V. Polevoda, Ph.D.

Bogdan V. Polevoda, Ph.D.

About Me

Faculty Appointments

Research Assistant Professor - Department of Biochemistry and Biophysics (SMD)

Credentials

Education

PhD | USSR - Free-Standing Inst. Genetics, All Other. 1986

MS | Ukraine-Inst/Type Unknown. Genetics. 1981

Research

Although there are only 20 primary amino acids that are encoded during translation, it is found that more than 100 different enzymatically modified amino acid residues are known from different proteins. The two cotranslational processes, cleavage of N-terminal methionine and N-terminal acetylation (...
Although there are only 20 primary amino acids that are encoded during translation, it is found that more than 100 different enzymatically modified amino acid residues are known from different proteins. The two cotranslational processes, cleavage of N-terminal methionine and N-terminal acetylation (N- acetylation), are by far the most common modifications, occurring on the vast majority of eukaryotic proteins.

N-acetylation is an enzyme-catalyzed reaction in which the protein N-terminal residues, such as a-Ser, a-Ala, a-Met, etc., accepts the acetyl group from acetyl-CoA. This modification neutralizes positive charges that may influence the protein function, stability, interaction with other molecules, or other subsequent modifications. The reaction is catalyzed by a number of acetyltransferases (NATs) that have been found in all kingdoms, prokaryotes, archaea and eukaryotes. N-acetylation is occurring on approximately 80-90% of the different varieties of cytosolic mammalian proteins, on about 50% of yeast proteins, but rarely on prokaryotic or archaeal proteins. It is believed that N-acetylation is cotranslational only in eukaryotes but not in prokaryotes, where it is posttranslational. In vitro studies indicated that NATs act on the newly synthesized polypeptide when there are between 25 to 50 residues extruding from the ribosome.

In our studies with yeast Saccharomyces cerevisiae we revealed that N-terminal protein acetylation occurs mainly by action of three NATs, NatA, NatB and NatC, which contain Ard1p, Nat3p and Mak3p catalytic subunits, respectively, and which act on groups of substrates, each containing degenerate motifs. NatA acetylates a subclasses of proteins with Ser-, Ala-, Gly- and Thr- termini; NatB acetylates Met-Glu- and Met-Asp- termini; and NatC acetylates a rare class of Met- termini. Recently, an additional NAT, Nat4p (NatD) was shown to acetylate the N-termini of histones H2A and H4, Ser-Gly-Gly-Lys-Gly- and Ser-Gly-Arg-Gly-Arg-, respectively. However, only subsets of proteins with any of these N-terminal residues are acetylated, and none of these residues guarantee acetylation, indicating that the enzymes recognize some structural characteristics of the N-terminal portion in addition to a particular amino acid sequence. Overall, the patterns of N-terminally acetylated proteins and orthologous genes possibly encoding NATs suggest that yeast and higher eukaryotes have the same or very similar system for N-terminal acetylation.

Three major NATs, NatA, NatB and NatC are heteromeric protein complexes containing at least one auxiliary subunit in addition to catalytic subunit, in contrast to NatD that appears to have no additional subunit. Interestingly, NatA contains two potential catalytic subunits, Ard1p and hypothetical acetyltransferase Nat5p, presumably with different substrate specificities. It has been shown recently that Nat1p is attached to the ribosome. In our experiments we demonstrated that Ard1p, Mak3p and Nat4p are cytoplasmic proteins, which were co-localized with polyribosomes in sucrose gradient. We suggested that the three auxiliary subunits, Nat1p, Mdm20p and Mak10p, may play a role in NAT attachment to the ribosome and recognition of a proper protein substrate.

Publications

Journal Articles

Csx28 is a membrane pore that enhances CRISPR-Cas13b-dependent antiphage defense.

VanderWal AR, Park JU, Polevoda B, Nicosia JK, Molina Vargas AM, Kellogg EH, O'Connell MR

Science.. 2023 April 28380 (6643):410-415. Epub 04/27/2023.

CRISPR-Csx28 forms a Cas13b-activated large-pore channel required for robust CRISPR-Cas immunity.

VanderWal AR, Park JU, Polevoda B, Nicosia JK, Molina Vargas AM, Kellogg EH, O'Connell MR

Biophysical journal.. 2023 February 10122 (3S1):194a. Epub 1900 01 01.

THUMPD1 bi-allelic variants cause loss of tRNA acetylation and a syndromic neurodevelopmental disorder.

Broly M, Polevoda BV, Awayda KM, Tong N, Lentini J, Besnard T, Deb W, O'Rourke D, Baptista J, Ellard S, Almannai M, Hashem M, Abdulwahab F, Shamseldin H, Al-Tala S, Alkuraya FS, Leon A, van Loon RLE, Ferlini A, Sanchini M, Bigoni S, Ciorba A, van Bokhoven H, Iqbal Z, Al-Maawali A, Al-Murshedi F, Ganesh A, Al-Mamari W, Lim SC, Pais LS, Brown N, Riazuddin S, Bézieau S, Fu D, Isidor B, Cogné B, O'Connell MR

American journal of human genetics.. 2022 February 11 Epub 02/11/2022.

Regulation of Antiviral Innate Immunity Through APOBEC Ribonucleoprotein Complexes.

Salter JD, Polevoda B, Bennett RP, Smith HC

Sub-cellular biochemistry.. 2019 93 :193-219. Epub 1900 01 01.

DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.

Polevoda B, Joseph R, Friedman AE, Bennett RP, Greiner R, De Zoysa T, Stewart RA, Smith HC

The Journal of biological chemistry.. 2017 May 26292 (21):8642-8656. Epub 04/05/2017.

Effects of an unusual poison identify a lifespan role for Topoisomerase 2 in .

Tombline G, Millen JI, Polevoda B, Rapaport M, Baxter B, Van Meter M, Gilbertson M, Madrey J, Piazza GA, Rasmussen L, Wennerberg K, White EL, Nitiss JL, Goldfarb DS

Aging.. 2017 January 59 (1):68-97. Epub 1900 01 01.

Structural and functional assessment of APOBEC3G macromolecular complexes.

Polevoda B, McDougall WM, Bennett RP, Salter JD, Smith HC

Methods : a companion to Methods in enzymology.. 2016 September 1107 :10-22. Epub 03/14/2016.

RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.

Polevoda B, McDougall WM, Tun BN, Cheung M, Salter JD, Friedman AE, Smith HC

Nucleic acids research.. 2015 October 3043 (19):9434-45. Epub 09/30/2015.

Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis.

Xu F, Huang Y, Li L, Gannon P, Linster E, Huber M, Kapos P, Bienvenut W, Polevoda B, Meinnel T, Hell R, Giglione C, Zhang Y, Wirtz M, Chen S, Li X

The Plant cell.. 2015 May 27 (5):1547-62. Epub 05/12/2015.

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R

Proceedings of the National Academy of Sciences of the United States of America.. 2012 July 31109 (31):12449-54. Epub 07/18/2012.

N(?)-Acetylation of yeast ribosomal proteins and its effect on protein synthesis.

Kamita M, Kimura Y, Ino Y, Kamp RM, Polevoda B, Sherman F, Hirano H

Journal of proteomics.. 2011 April 174 (4):431-41. Epub 12/22/2010.

A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates.

Polevoda B, Arnesen T, Sherman F

BMC proceedings.. 2009 August 43 Suppl 6 (Suppl 6):S2. Epub 08/04/2009.

Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.

Polevoda B, Hoskins J, Sherman F

Molecular and cellular biology.. 2009 June 29 (11):2913-24. Epub 03/30/2009.

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans.

Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, Varhaug JE, Vandekerckhove J, Lillehaug JR, Sherman F, Gevaert K

Proceedings of the National Academy of Sciences of the United States of America.. 2009 May 19106 (20):8157-62. Epub 05/06/2009.

Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes.

Polevoda B, Brown S, Cardillo TS, Rigby S, Sherman F

Journal of cellular biochemistry.. 2008 February 1103 (2):492-508. Epub 1900 01 01.

Methylation of proteins involved in translation.

Polevoda B, Sherman F

Molecular microbiology.. 2007 August 65 (3):590-606. Epub 07/04/2007.

The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p.

Polevoda B, Span L, Sherman F

The Journal of biological chemistry.. 2006 February 3281 (5):2562-71. Epub 12/01/2005.

Phenotypes of yeast mutants lacking the mitochondrial protein Pet20p.

Polevoda B, Panciera Y, Brown SP, Wei J, Sherman F

Yeast.. 2006 January 3023 (2):127-39. Epub 1900 01 01.

Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin.

Polevoda B, Cardillo TS, Doyle TC, Bedi GS, Sherman F

The Journal of biological chemistry.. 2003 August 15278 (33):30686-97. Epub 06/03/2003.

Composition and function of the eukaryotic N-terminal acetyltransferase subunits.

Polevoda B, Sherman F

Biochemical and biophysical research communications.. 2003 August 15308 (1):1-11. Epub 1900 01 01.

N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins.

Polevoda B, Sherman F

Journal of molecular biology.. 2003 January 24325 (4):595-622. Epub 1900 01 01.

N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome.

Kimura Y, Saeki Y, Yokosawa H, Polevoda B, Sherman F, Hirano H

Archives of biochemistry and biophysics.. 2003 January 15409 (2):341-8. Epub 1900 01 01.

The diversity of acetylated proteins.

Polevoda B, Sherman F

Genome biology.. 2002 3 (5):reviews0006. Epub 04/30/2002.

NatC Nalpha-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p.

Polevoda B, Sherman F

The Journal of biological chemistry.. 2001 June 8276 (23):20154-9. Epub 03/27/2001.

Nalpha -terminal acetylation of eukaryotic proteins.

Polevoda B, Sherman F

The Journal of biological chemistry.. 2000 November 24275 (47):36479-82. Epub 1900 01 01.

Cytochrome c methyltransferase, Ctm1p, of yeast.

Polevoda B, Martzen MR, Das B, Phizicky EM, Sherman F

The Journal of biological chemistry.. 2000 July 7275 (27):20508-13. Epub 1900 01 01.

N(alpha)-acetylation and proteolytic activity of the yeast 20 S proteasome.

Kimura Y, Takaoka M, Tanaka S, Sassa H, Tanaka K, Polevoda B, Sherman F, Hirano H

The Journal of biological chemistry.. 2000 February 18275 (7):4635-9. Epub 1900 01 01.

Induced G2/M arrest and apoptosis in human epidermoid carcinoma cell lines by semisynthetic drug Ukrain.

Roublevskaia IN, Polevoda BV, Ludlow JW, Haake AR

Anticancer research.. 2000 20 (5A):3163-7. Epub 1900 01 01.

Induced apoptosis in human prostate cancer cell line LNCaP by Ukrain.

Roublevskaia IN, Haake AR, Ludlow JW, Polevoda BV

Drugs under experimental and clinical research. 2000 26 (5-6):141-7. Epub 1900 01 01.

Bcl-2 overexpression protects human keratinocyte cells from Ukrain-induced apoptosis but not from G2/M arrest.

Roublevskaia IN, Haake AR, Polevoda BV

Drugs under experimental and clinical research. 2000 26 (5-6):149-56. Epub 1900 01 01.

The action of N-terminal acetyltransferases on yeast ribosomal proteins.

Arnold RJ, Polevoda B, Reilly JP, Sherman F

The Journal of biological chemistry.. 1999 December 24274 (52):37035-40. Epub 1900 01 01.

Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae.

Polevoda B, Norbeck J, Takakura H, Blomberg A, Sherman F

The EMBO journal.. 1999 November 118 (21):6155-68. Epub 1900 01 01.

Neuronal overexpression of heme oxygenase-1 correlates with an attenuated exploratory behavior and causes an increase in neuronal NADPH diaphorase staining.

Maines MD, Polevoda B, Coban T, Johnson K, Stoliar S, Huang TJ, Panahian N, Cory-Slechta DA, McCoubrey WK

Journal of neurochemistry.. 1998 May 70 (5):2057-69. Epub 1900 01 01.

Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes.

Maines MD, Polevoda BV, Huang TJ, McCoubrey WK

European journal of biochemistry. 1996 January 15235 (1-2):372-81. Epub 1900 01 01.

[The genetic aspects of the study of Pseudomonas syringae bacteria].

Perepnikhatka VI, Polevoda BV

Mikrobiolohichny? zhurnal. = Mikrobiologichny zhurnal.. 1995 57 (3):84-97. Epub 1900 01 01.

[The stability of plasmid pSG 1912 inheritance by the cells of Streptomyces globisporus 1912 and of heterologous streptomycete strains].

Polishchuk LV, Polevoda BV, Zaverukha VB, Matseliukh BP

Mikrobiologicheski? zhurnal. 1992 54 (3):9-14. Epub 1900 01 01.

[The cloning of fragments of the streptomycete plasmid pSG1912 as a part of the vector pUC19].

Zaverukha VB, Polevoda BV, Polishchuk LV, Matseliukh BP

Mikrobiologicheski? zhurnal. 1992 54 (5):30-5. Epub 1900 01 01.

[Mapping of the regions participating in the replication, maintenance and mobilization of the R-plasmid pBS222 with a wide circle of bacterial hosts].

Polevoda BV, Gribanova LK, Ugarov VI, Lebedev AN, Tso? TV

Genetika.. 1988 March 24 (3):405-13. Epub 1900 01 01.

[Molecular genetic organization and origin of plasmid pBS52 with a broad range of bacterial hosts].

Polevoda BV, Tso? TV, Boronin AM

Genetika.. 1987 October 23 (10):1823-31. Epub 1900 01 01.

[Structural-functional organization of R-plasmid pBS222 with a broad range of bacterial hosts].

Polevoda BV, Tso? TV, Boronin AM

Molekuliarnaia genetika, mikrobiologiia i virusologiia. 1986 December (12):3-10. Epub 1900 01 01.

[Genetic characteristics and physical organization of the R-plasmid pBS52 with a broad range of bacterial hosts].

Polevoda BV, Tso? TV, Boronin AM

Molekuliarnaia genetika, mikrobiologiia i virusologiia. 1986 November (11):18-23. Epub 1900 01 01.

[Comparative study of non-conjugative R-plasmids from enterobacteria and Pseudomonas aeruginosa].

Anisimova LA, Viatkina GG, Polevoda BV, Korotiaev AI, Boronin AM

Molekuliarnaia genetika, mikrobiologiia i virusologiia. 1985 June (6):24-8. Epub 1900 01 01.

[Restriction analysis of hybrid plasmids pESO1-2 and pESG1-2].

Stefanishin EE, Dekhtiarenko TD, Polishchuk LV, Polevoda BV

Mikrobiologicheski? zhurnal. 1983 45 (2):40-3. Epub 1900 01 01.