Juha A. E. Määttä

ORCID: 0000-0003-3885-6149
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About
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Research Areas
  • Biotin and Related Studies
  • Molecular Junctions and Nanostructures
  • Click Chemistry and Applications
  • Monoclonal and Polyclonal Antibodies Research
  • Cellular transport and secretion
  • RNA and protein synthesis mechanisms
  • Viral Infections and Immunology Research
  • Advanced Biosensing Techniques and Applications
  • Cell Adhesion Molecules Research
  • RNA regulation and disease
  • Cellular Mechanics and Interactions
  • Protein Structure and Dynamics
  • Advanced biosensing and bioanalysis techniques
  • Nanofabrication and Lithography Techniques
  • Vitamin D Research Studies
  • Sirtuins and Resveratrol in Medicine
  • Viral gastroenteritis research and epidemiology
  • Endoplasmic Reticulum Stress and Disease
  • Force Microscopy Techniques and Applications
  • Air Quality and Health Impacts
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Plant biochemistry and biosynthesis
  • Calpain Protease Function and Regulation
  • Occupational exposure and asthma
  • Aquaculture disease management and microbiota

Tampere University
2014-2024

Fimlab (Finland)
2012-2023

Tampere University Hospital
2008-2019

FIT Biotech (Finland)
2011-2014

Tampere University of Applied Sciences
2008-2014

Pirkanmaa Hospital District
2013

University of Jyväskylä
2004-2007

Lappeenranta-Lahti University of Technology
2006

Finnish Institute of Occupational Health
2004

University of Helsinki
2000

Abstract The protein phosphatase 2A (PP2A) heterotrimer PP2A-B56α is a human tumour suppressor. However, the molecular mechanisms inhibiting in cancer are poorly understood. Here, we report level details and structural of inhibition by an oncoprotein CIP2A. Upon direct binding to trimer, CIP2A displaces PP2A-A subunit thereby hijacks both B56α, catalytic PP2Ac form CIP2A-B56α-PP2Ac pseudotrimer. Further, competes with B56α substrate blocking LxxIxE-motif pocket on B56α. Relevant oncogenic...

10.1038/s41467-023-36693-9 article EN cc-by Nature Communications 2023-02-28

Rhizobium etli CFN42 is a symbiotic nitrogen-fixing bacterium of the common bean Phaseolus vulgaris. The plasmid p42d R. comprises gene encoding putative (strept)avidin-like protein, named rhizavidin. amino acid sequence identity rhizavidin in relation to other known avidin-like proteins 20–30%. residues involved (strept)avidin–biotin interaction are well conserved structural and functional properties were carefully studied, we found that shares characteristics with bradavidin, streptavidin...

10.1042/bj20070076 article EN Biochemical Journal 2007-07-13

Integrin-dependent cell adhesion and spreading are critical for morphogenesis, tissue regeneration, immune defense but also tumor growth. However, the mechanisms that induce integrin-mediated provide mechanosensing on different extracellular matrix conditions not fully understood. By expressing β3-GFP-integrins with enhanced talin-binding affinity, we experimentally uncoupled integrin activation, clustering, substrate binding from its function in spreading. Mutational analysis revealed...

10.1083/jcb.201308136 article EN cc-by-nc-sa The Journal of Cell Biology 2014-04-28

Chicken avidin is a highly popular tool with countless applications in the life sciences. In present study, an efficient method for producing protein periplasmic space of Escherichia coli active form described. Avidin was produced by replacing native signal sequence bacterial OmpA secretion signal. The yield after single 2-iminobiotin–agarose affinity purification step approx. 10 mg/l virtually pure avidin. Purified had 3.7 free biotin-binding sites per tetramer and showed same thermal...

10.1042/bj20041114 article EN Biochemical Journal 2004-11-23

Significance Although efforts have been made to determine the structure of talin and way it interacts with integrins through “head” domain, our work shows now that many previous mechanistic models based on adapter are likely be misleading as they constructed a crystal representing an improperly folded head domain. In this work, we identified problem current model proposed FERM-folded head. By analyzing these structural features in cellular context, involving also kindlin adapter, making...

10.1073/pnas.2014583117 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2020-12-07

Avidin and its bacterial analog streptavidin have been widely used in applications life sciences. Recently, we described a highly thermostable engineered avidin, called chimeric which is hybrid of avidin avidin-related protein 4. Here, report protocol for pilot-scale production E. coli the X-ray structure avidin. The ligand-binding properties were explored with isothermal titration calorimetry. We found to be more stable against various harsh organic solvents at elevated temperatures...

10.1002/bit.22962 article EN Biotechnology and Bioengineering 2010-10-11

Switchavidin is a chicken avidin mutant displaying reversible binding to biotin, an improved affinity toward conjugated and low nonspecific due reduced surface charge. These properties make switchavidin optimal tool in biosensor applications for the immobilization of biotinylated proteins on sensor surfaces. Furthermore, opens novel possibilities patterning, purification, labeling.

10.1021/bc500462w article EN Bioconjugate Chemistry 2014-11-18

BACKGROUND: Respiratory symptoms, impaired lung function, and asthma have been reported in workers exposed to wood dust a number of epidemiological studies. The underlying pathomechanisms, however, are not well understood. Here, we studied the effects from pine (PD) heat-treated (HPD) on release reactive oxygen species (ROS) inflammatory mediators rat alveolar macrophages. METHODS: Tumour necrosis factor-alpha (TNF-alpha) macrophage protein-2 (MIP-2) protein release, TNF-alpha MIP-2 mRNA...

10.1186/1743-8977-1-3 article EN cc-by Particle and Fibre Toxicology 2004-12-13

Repeated airway exposure to wood dust has long been known cause adverse respiratory effects such as asthma and chronic bronchitis impairment of lung function. However, the mechanisms underlying inflammatory responses airways after are poorly known. We used a mouse model elucidate particle-induced fine particles. BALB/c mice were exposed intranasally administered (more than 99% particles had particle size ≤ 5 μm, with virtually identical distribution) birch or oak dusts twice week for 3...

10.1093/toxsci/kfl026 article EN Toxicological Sciences 2006-06-01

scAvd (single-chain avidin, where two dcAvd are joined in a single polypeptide chain), having four biotin-binding domains, was constructed by fusion of topologically modified avidin units. showed similar biotin binding and thermal stability properties as chicken avidin. The DNA construct encoding contains circularly permuted plus short linkers connecting the domains into chain. In contrast with wild-type which identical monomers, enables each one to be independently protein engineering....

10.1042/bj20051038 article EN Biochemical Journal 2005-12-06

Abstract Background Avidins are proteins with extraordinarily high ligand-binding affinity, a property which is used in wide array of life science applications. Even though useful for biotechnology and nanotechnology, the biological function avidins not fully understood. Here we structurally functionally characterise novel avidin named xenavidin, to our knowledge first reported from frog. Results Xenavidin was identified an EST sequence database Xenopus tropicalis produced insect cells using...

10.1186/1472-6807-9-63 article EN cc-by BMC Structural Biology 2009-09-29

The murine inhibitor of carbonic anhydrase (mICA), a member the transferrin (TF) superfamily proteins, together with human holo- and apoTF lactoferrin (LF) were assessed as inhibitors all catalytically active mammalian (h = human, m murine) CA isoforms, from I to XV. mICA was low nanomolar subnanomolar hCAs I, II, III, VA, VB, VII mCAs XV (KI 0.7–44.0 nM) inhibited remaining isoforms KI 185.5–469 nM. hTF, apoTF, hLF most these CAs but reduced efficiency compared 18.9–453.8 nM). Biacore...

10.1021/jm3004587 article EN Journal of Medicinal Chemistry 2012-05-11

ABSTRACT Integrin activation and clustering by talin are early steps of cell adhesion. Membrane-bound head domain kindlin bind to the β integrin cytoplasmic tail, cooperating activate heterodimeric integrin, induces in presence Mn2+. Here we show that kindlin-1 can replace Mn2+ mediate β3 induced head, but not F2–F3 fragment talin. mediated was lost upon deletion flexible loop within F1 subdomain. Further mutagenesis identified hydrophobic acidic motifs responsible for clustering. Modeling,...

10.1242/jcs.239202 article EN Journal of Cell Science 2020-10-01

Abstract Chicken avidin is a key component used in wide variety of biotechnological applications. Here we present circularly permuted (cpAvd4→3) that lacks the loop between β‐strands 3 and 4. Importantly, deletion has positive effect on binding 4′‐hydroxyazobenzene‐2‐carboxylic acid (HABA) to avidin. To increase HABA affinity cpAvd4→3 even further, mutated asparagine 118 bottom ligand‐binding pocket methionine, which simultaneously caused significant drop biotin‐binding affinity. The X‐ray...

10.1002/cbic.200700671 article EN ChemBioChem 2008-04-01

The avidin protein family members are well known for their high affinity towards D-biotin and structural stability. These properties make avidins valuable tools a wide range of biotechnology applications. We have identified new member the in zebrafish (Danio rerio) genome, hereafter called zebavidin. is highly expressed gonads both male female gills fish, but our data suggest that zebavidin not crucial developing embryo. Biophysical characterisation revealed distinct found any previously...

10.1371/journal.pone.0077207 article EN cc-by PLoS ONE 2013-10-24

Abstract Background The chicken avidin gene family consists of and several related genes ( AVR s). Of these products, is the best characterized known for its extremely high affinity D-biotin, a property that utilized in numerous modern life science applications. Recently, have been expressed as recombinant proteins, which shown different biotin-binding properties compared to avidin. Results In present study, we employed multiple biochemical methods better understand structure-function...

10.1186/1472-6750-5-28 article EN cc-by BMC Biotechnology 2005-10-07

Bradavidin II is a biotin-binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, isothermal titration calorimetry combined with structural X-ray crystallography. These observations revealed bradavidin differs canonical homotetrameric family members in its quaternary structure. In contrast the other...

10.1002/pro.2281 article EN Protein Science 2013-05-10

The modulation of protein deacetylase SIRT1 has a vast therapeutic potential in treatment several aging-associated diseases. Active regulator (AROS) is small endogenous which was originally reported to activate through direct interaction cancer cells. We show that the between two proteins weak and does not alter activity non-cancerous human results different vitro assays disclosed AROS as an inhibitor SIRT1. functional relationship proved be dependent on biological context experimental setting.

10.1016/j.febslet.2014.03.020 article EN FEBS Letters 2014-03-26
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