Cecilia Blikstad

ORCID: 0000-0001-5740-926X
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About
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Research Areas
  • Microbial Metabolic Engineering and Bioproduction
  • Photosynthetic Processes and Mechanisms
  • Enzyme Catalysis and Immobilization
  • Enzyme Structure and Function
  • Algal biology and biofuel production
  • Ubiquitin and proteasome pathways
  • Protein Structure and Dynamics
  • Microbial bioremediation and biosurfactants
  • Bacterial Genetics and Biotechnology
  • Peptidase Inhibition and Analysis
  • Microbial Community Ecology and Physiology
  • Enzyme function and inhibition
  • Advanced Proteomics Techniques and Applications
  • Biochemical and Molecular Research
  • Amino Acid Enzymes and Metabolism
  • ATP Synthase and ATPases Research
  • Signaling Pathways in Disease
  • Advanced Electron Microscopy Techniques and Applications
  • Genomics and Phylogenetic Studies
  • Chemical Reactions and Mechanisms
  • Microbial Fuel Cells and Bioremediation
  • Cancer Research and Treatments
  • CO2 Reduction Techniques and Catalysts
  • Endoplasmic Reticulum Stress and Disease
  • Diatoms and Algae Research

Uppsala University
2013-2025

University of California, Berkeley
2018-2023

Many photosynthetic organisms employ a CO 2 concentrating mechanism (CCM) to increase the rate of fixation via Calvin cycle. CCMs catalyze ≈50% global photosynthesis, yet it remains unclear which genes and proteins are required produce this complex adaptation. We describe construction functional CCM in non-native host, achieved by expressing from an autotrophic bacterium Escherichia coli strain engineered depend on rubisco carboxylation for growth. Expression 20 enabled E. grow fixing...

10.7554/elife.59882 article EN cc-by eLife 2020-10-21

The intrinsically disordered regions of eukaryotic proteomes are enriched in short linear motifs (SLiMs), which crucial relevance for cellular signaling and protein regulation; many mediate interactions by providing binding sites peptide-binding domains. vast majority SLiMs remain to be discovered highlighting the need experimental methods their large-scale identification. We present a novel proteomic peptide phage display (ProP-PD) library that displays peptides representing human proteome,...

10.1111/febs.13995 article EN cc-by FEBS Journal 2016-12-21

Despite the importance of microcompartments in prokaryotic biology and bioengineering, structural heterogeneity has prevented a complete understanding their architecture, ultrastructure, spatial organization. Here, we employ cryo-electron tomography to image α-carboxysomes, pseudo-icosahedral microcompartment responsible for carbon fixation. We have solved high-resolution subtomogram average Rubisco cargo inside carboxysome, determined arrangement enzyme. find that H. neapolitanus...

10.1038/s41467-022-32584-7 article EN cc-by Nature Communications 2022-08-18

Carboxysomes are proteinaceous organelles that encapsulate key enzymes of CO 2 fixation—Rubisco and carbonic anhydrase—and the centerpiece bacterial concentrating mechanism (CCM). In CCM, actively accumulated cytosolic bicarbonate diffuses into carboxysome is converted to by anhydrase, producing a high concentration near Rubisco ensuring efficient carboxylation. Self-assembly α-carboxysome orchestrated intrinsically disordered scaffolding protein, CsoS2, which interacts with both...

10.1073/pnas.2308600120 article EN cc-by Proceedings of the National Academy of Sciences 2023-10-20

Interactions between modular domains and short linear motifs (3–10 amino acids peptide stretches) are crucial for cell signaling. The typically reside in the disordered regions of proteome interactions often transient, allowing rapid changes response to changing stimuli. properties that make domain-motif suitable signaling also them difficult capture experimentally they therefore largely underrepresented known protein-protein interaction networks. Most knowledge on is derived from...

10.1186/s12964-015-0116-8 article EN cc-by Cell Communication and Signaling 2015-08-21

Hub proteins participate in cellular regulation by dynamic binding of multiple within interaction networks. The hub protein LC8 reversibly interacts with more than 100 partners through a flexible pocket at its dimer interface. To explore the diversity partner pool, we screened for using proteomic phage display library composed peptides from human proteome, which had no bias toward known motif. Of identified hits, validated 29 isothermal titration calorimetry. peptides, 19 were entirely...

10.26508/lsa.201900366 article EN cc-by Life Science Alliance 2019-07-02

This study investigated the structural basis of adenosine triphosphate (ATP) release and ion selectivity by Pannexin1 (Panx1). The microinjection active SRC tyrosine kinase increased Panx1-mediated currents in Panx1-expressing oocytes. Furthermore, a mutation mimicking phosphorylation at Y308 turned Panx1 into constitutively open ATP-releasing channel with broad permeability. Cryogenic electron microscopy showed that for most maps, alternated between wide narrow conformations. However, map...

10.1101/2025.02.17.638584 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2025-02-20

Abstract Isobutene is a promising precursor for jet fuel due to its high energy density and favorable combustion properties. Light-driven bioproduction of isobutene has recently been investigated as an alternative strategy crude oil refinement or fermentation-based manufacturing processes by harnessing the unicellular cyanobacterium Synechocystis sp. PCC 6803 α-ketoisocaproate dioxygenase ( Rn KICD) from Rattus norvegicus . However, obtained production level was not sufficient, partially...

10.1186/s12934-025-02708-x article EN cc-by Microbial Cell Factories 2025-04-23

α-Hydroxy aldehydes are chiral building blocks used in synthesis of natural products and synthetic drugs. One route to their production is by regioselective oxidation vicinal diols and, this work, we aimed perform the 3-phenyl-1,2-propanediol into corresponding α-hydroxy aldehyde applying enzyme catalysis. Propanediol oxidoreductase from Escherichia coli efficiently catalyzes stereoselective S-1,2-propanediol S-lactaldehyde. The enzyme, however, shows no detectable activity with...

10.1021/cs400824h article EN ACS Catalysis 2013-11-04

We have analyzed the effects of mutations inserted during directed evolution a specialized enzyme, Escherichia coli S-1,2-propanediol oxidoreductase (FucO). The kinetic properties evolved variants been determined and observed differences rationalized by modeling tertiary structures isolated wild-type enzyme. native substrate, S-1,2-propanediol, as well phenylacetaldehyde 2S-3-phenylpropane-1,2-diol, which are new substrates accepted variants, were docked into active sites. study provides...

10.1111/febs.12791 article EN FEBS Journal 2014-03-26

ABSTRACT Carboxysomes are proteinaceous organelles that encapsulate key enzymes of CO 2 fixation - Rubisco and carbonic anhydrase the centerpiece bacterial concentrating mechanism (CCM). In CCM, actively accumulated cytosolic bicarbonate diffuses into carboxysome is converted to by anhydrase, producing a high concentration near ensuring efficient carboxylation. Self-assembly α-carboxysome orchestrated intrinsically disordered scaffolding protein, CsoS2, which interacts with both carboxysomal...

10.1101/2021.11.05.467472 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2021-11-05

Abstract Isobutene is a promising precursor for jet fuel due to its high energy density and favorable combustion properties. Light-driven bioproduction of isobutene has recently been investigated as an alternative strategy crude oil refinement or fermentation-based manufacturing processes by harnessing the unicellular cyanobacterium Synechocystis sp. PCC 6803 α-ketoisocaproate dioxygenase ( Rn KICD) from Rattus norvegicus . However, obtained production level was not sufficient, partially...

10.1101/2024.12.20.629387 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-12-25

Bacteria employ microcompartments to sequester enzymatic processes, either for purposes of protecting cellular contents from reactive intermediates or as a way increasing reaction efficiency. In these structures, cargo enzymes and accessory proteins is encased within semi-permeable protein shell that permits passage substrates products but restricts movement intermediates. addition their importance component many bacterial species’ metabolisms, have recently become target engineering. The...

10.1101/2022.01.24.477598 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-01-25

Structural and biochemical studies of the orf12 gene product (ORF12) from clavulanic acid (CA) biosynthesis cluster are described. Sequence crystallographic analyses reveal two domains: a C-terminal penicillin-binding protein (PBP)/β-lactamase-type fold with highest structural similarity to class A β-lactamases fused an N-terminal domain similar steroid isomerases polyketide cyclases. The ORF12 did not show β-lactamase or PBP activity for substrates tested, but low-level esterase towards...

10.1107/s0907444913011013 article EN Acta Crystallographica Section D Biological Crystallography 2013-07-19

Summary Short linear motifs (SLiMs) drive dynamic protein-protein interactions essential for signaling, but sequence degeneracy and low binding affinities make them difficult to identify. We harnessed unbiased systematic approaches SLiM discovery elucidate the regulatory network of calcineurin (CN)/PP2B, Ca 2+ -activated phosphatase that recognizes LxVP PxIxIT motifs. In vitro proteome-wide detection CN-binding peptides, in vivo SLiM-dependent proximity labeling, silico modeling motif...

10.1101/632547 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2019-05-09

10.1016/bs.mie.2024.10.012 article EN Methods in enzymology on CD-ROM/Methods in enzymology 2024-01-01

Abstract Many bacterial autotrophs rely on CO 2 concentrating mechanisms (CCMs) to assimilate carbon. Although many CCM proteins have been identified, including a 200+ MDa protein organelle called the carboxysome, systematic screen of components has not carried out. Here, we performed genome-wide barcoded transposon identify essential and CCM-related genes in ɣ-proteobacterium H. neapolitanus . Our revealed an operon critical for function which encodes domain unknown (PFAM:PF10070) putative...

10.1101/476713 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2018-11-22

Abstract Many photosynthetic organisms employ a CO 2 concentrating mechanism (CCM) to increase the rate of fixation via Calvin cycle. CCMs catalyze ≈50% global photosynthesis, yet it remains unclear which genes and proteins are required produce this complex adaptation. We describe construction functional CCM in non-native host, achieved by expressing from an autotrophic bacterium engineered E. coli strain. Expression 20 enabled grow fixing ambient air into biomass, with growth depending on...

10.1101/2020.05.27.119784 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-05-27
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