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Appendix 3 Review of Selected Papers and Discussion of the Research And Appendix 3 Review of selected papers and discussion of the research and other achievements Liliana Surmacz, PhD Institute of Biochemistry and Biophysics Polish Academy of Sciences Department of Lipid Biochemistry Pawińskiego 5a 02-106 Warsaw, Poland Warsaw 2017 Appendix 3 L. Surmacz 1. Name and surname: Liliana Surmacz 2. Diplomas, scientific degrees held - including the name, place and year of acquisition and the title of the doctoral dissertation: 2004 Ph.D. in Biology - Molecular Biology, Nencki Institute of Experimental Biology PAS in Warsaw, The title of Ph.D. thesis „Rab7 in Paramecium cells: studies on gene, protein and localization during endocytosis”, Supervisor: Prof. Elżbieta Wyroba 1995 M.Sc. in Biology - Microbiology, University of Lodz, Faculty of Biology and Earth Sciences, The title of M.Sc. thesis: „The use of an enzyme immunoassay APAAP for the identification of markers that differentiate human lymphocytes”, Supervisor: Prof. Wiesława Rudnicka 3. Information on employment in scientific institutions: science 10. 2006 till present Assistant Professor at the Department of Lipid Biochemistry, Institute of Biochemistry and Biophysics PAS, Warsaw, Poland. 09.2008 – 05.2010 maternity leave 09.2006 – 10.2006 biologist at the Department of Lipid Biochemistry, Institute of Biochemistry and Biophysics PAS, Warsaw, Poland. 12.1995 – 08.2006 assistant at the Laboratory of Cell Membrane Physiology, the Nencki Institute of Experimental Biology PAS, Warsaw, Poland 01.1998 – 01.2000 maternity leave 4. Description of the achievement under the Article 16.2 of the Act of 14 March 2003 on academic degrees and academic title and degrees and title in art (Journal of Laws, item 882, 2016 and item 1311, 2016): a) title of the scientific achievement, The scientific achievement consists of five papers published in the journals listed by the Journal Citation Report, total IF matching the year of publication is: 26.581 (WoS); total points (according to the list of the Ministry of Science and Higher Education, MSHE): 180; times cited: 58 (WoS). Polyisoprenoids as eukaryotic "superlipids" - characteristic of mechanisms of biosynthesis and the search for cellular functions. b) authors, title of publication, year of publication, name of publisher: 1. Surmacz L*, Swiezewska E. (2011) Polyisoprenoids - Secondary metabolites or physiologically important superlipids? Biochem Biophys Res Commun. 407, 627-632. IF2011: 2.484 (WoS); 20 points (MSHE); times cited: 37 (WoS) 2 Appendix 3 L. Surmacz 2. Surmacz L*, Plochocka D, Kania M, Danikiewicz W, Swiezewska E. (2014) cis-Prenyltransferase AtCPT6 produces a family of very short-chain polyisoprenoids in planta. Biochim Biophys Acta. 1841, 240-250. IF2014: 5.162; (WoS); 35 points (MSHE); times cited: 10 (WoS) 3. Akhtar TA*, Surowiecki P, Siekierska H, Kania M, Van Gelder K, Rea KA, Virta LKA, Vatta M, Gawarecka K, Wojcik J, Danikiewicz W, Buszewicz D, Swiezewska E, Surmacz L* (2017) Polyprenols are synthesized by a plastidial cis-prenyltransferase and influence photosynthetic performance. Plant Cell, 29, 1709-1725. IF2016: 8.688 (WoS); 45 points (MSHE); times cited: 1 (WoS) 4. Brasher MI, Surmacz L, Leong B, Pitcher J, Swiezewska E, Pichersky E, Akhtar TA.(2015) A two-component enzyme complex is required for dolichol biosynthesis in tomato. Plant J. 82, 903- 914. IF2015: 5.468 (WoS); 45 points (MSHE); times cited: 9 (WoS) 5. Surmacz L*, Wojcik J, Kania M, Bentinger M, Danikiewicz W, Dallner G, Surowiecki P, Cmoch P, Swiezewska E. (2015) Short-chain polyisoprenoids in the yeast Saccharomyces cerevisiae - New companions of the old guys. Biochim Biophys Acta 1851, 1296-1303. IF2015: 4.779 (WoS); 35 points (MSHE); times cited: 1 (WoS) *corresponding author c) presentation of the scientific objectives of the publications listed above, the results obtained, and possible applications The scientific achievement is a collection of five thematically closely related papers presenting the results of my studies performed at the Department of Lipid Biochemistry, Institute of Biochemistry and Biophysics Polish Academy of Sciences. The main objective of the studies summarized herein was the identification, molecular characterization and elucidation of the cellular role of enzymes involved in polyisoprenoid biosynthesis. These studies were motivated by the vital role polyisoprenoid lipids play in the cells (among others as obligate cofactors of protein glycosylation) and concomitantly by the extremely limited knowledge on their biosynthetic mechanisms, especially in plant cells. When performing this project I cooperated with research groups from Poland and abroad, i.e. the group of Prof. Witold Danikiewicz from the Institute of Organic Chemistry of the Polish Academy of Sciences in Warsaw and the group of Dr. Tariq Akhtar from the University of Guelph, Canada. Studies described in the papers constituting the presented scientific achievement were financially supported by the projects submitted by me and performed under my leadership: POL-POSTDOC II grant "The role of protein prenylation and prenylated lipids in the vesicular transport in plants” provided by the Polish 3 Appendix 3 L. Surmacz Ministry of Science and Higher Education (2006 – 2011) and National Centre of Science OPUS 2 grant "Implications of gene multiplicity of Arabidopsis cis-prenyltransferases on the polyisoprenoid alcohols biosynthesis and plant stress tolerance" (2012 – 2016). Polyisoprenoid alcohols are biopolymers present in the cells of all living organisms. Despite the fact that polyisoprenoids have been studied extensively for more than 50 years, our knowledge of their properties, the mechanisms of biosynthesis and their role in the cell is still far from being complete. Polyisoprenoids have important biological functions during protein post- and co-translational modifications, namely they serve as obligate cofactors in the biosynthesis of glycosyl-phosphoinositol (GPI) anchor and protein N-, O- and C-glycosylation [Burda et al., 1999; Pattison et al., 2009; Nothaft at al., 2010] as well as donors of isoprenoid groups in protein prenylation [Swiezewska et al., 1993]. Moreover, they are implicated in cell adaptation to adverse environmental conditions [Bajda et al., 2009] possibly via modulation of the properties of biological membranes by increasing their permeability and fluidity and enhancing membrane fusion [summarized in Swiezewska and Danikiewicz, 2005]. Importantly, mutations in genes encoding enzymes of the polyisoprenoid biosynthesis pathway lead to severe metabolic disorders in humans (CDG, Congenital Disorders of Glycosylation type I) [summarized in Buczkowska et al., 2015] while some of them are lethal in plants [summarized in Hemmerlin et al., 2012]. Polyisoprenoid alcohols found in cells vary in their chain length - depending on the origin polyisoprenoid chains consist of from 5 to more than 100 isoprene residues, with a hydroxyl group at one end and hydrogen at the other (α- and ω-isoprene residue, respectively) [Swiezewska and Danikiewicz, 2005]. Depending on the presence of the double bond in the α-isoprene residue, these compounds are subdivided into polyprenols (α-unsaturated, Pren) and dolichols (α-saturated, Dol). Polyprenols occur mainly in bacteria cells and plant photosynthetic tissues whereas dolichols - in animal and yeast cells and in plant roots. It is worth underlining that in eukaryotic cells dolichols and polyprenols are always found as mixtures of homologues (named ‘families’), moreover, dolichols are accompanied by traces of polyprenols of the same chain-length. Polyisoprenoids are accumulated in the form of free alcohols and/or esters of carboxylic acids along with a small fraction of mono- and diphosphates. The content of polyisoprenoids increases during the life span of organisms and upon pathological conditions or environmental stress. Based on the configuration of the double bonds polyisoprenoid alcohols are classified into three main groups: 1) di-trans-poly-cis – bactoprenol (in most bacteria composed of 11 isoprene units) and plant polyprenols containing 5-9 isoprene units (i.u.) or more than 16 i.u. and animal, yeast and plant dolichols 2) tri-trans-poly-cis – polyprenols containing 9-15 i.u. 4 Appendix 3 L. Surmacz 3) all-trans – solanesol (all-trans Pren-9) isolated from Solanaceae plants [Hemming, 1983] and all- trans Pren-7 from Saccharomyces cerevisiae [Surmacz et al, 2015], oligoprenols: geraniol (2 i.u.), farnesol (3 i.u.) and geranylgeraniol (4 i.u.) also belong to this group. Biosynthesis of polyisoprenoids occurs in three steps: 1) Formation of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) – five- carbon precursors of isoprenoids; 2) Elongation of polyisoprenoid chain by subsequent condensation of IPP molecules to obtain polyprenyl diphosphate/polyprenol; 3) Reduction of the double bond in the α residue of polyprenol to form dolichol. Step 1. All isoprenoids are formed from the common precursor, isopentenyl diphosphate (IPP), which in plants is synthesized via two pathways operating in parallel: the mevalonate (MVA) and the methylerythritol phosphate (MEP) pathway. Both IPP-generating pathways are compartmentalized in plant cells - the enzymes of the MVA pathway are present in the cytoplasm whereas those of the MEP pathway – in plastids [summarized in Hemmerlin et al., 2012]. In contrast to plant cells, in archaebacteria [Smit and Mushegian, 2000], some gram-positive bacteria [Wilding et al., 2000], yeasts [Denbow et al., 1996] and animals [Kovacs et al., 2002] IPP
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