liu.seSearch for publications in DiVA
Change search
Link to record
Permanent link

Direct link
BETA
Jonsson, Bengt-Harald
Alternative names
Publications (10 of 58) Show all publications
Babu Moparthi, S., Carlsson, U., Vincentelli, R., Jonsson, B.-H., Hammarström, P. & Wenger, J. (2016). Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components. Scientific Reports, 6(28386)
Open this publication in new window or tab >>Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components
Show others...
2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, no 28386Article in journal (Refereed) Published
Abstract [en]

Here, we study and compare the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from E. coli. MreB is a homologue to actin in prokaryotes. Single-molecule fluorescence correlation spectroscopy (FCS) and time-resolved fluorescence polarization anisotropy report the binding interaction of folding MreB with GroEL, GroES and TRiC. Fluorescence resonance energy transfer (FRET) measurements on MreB variants quantified molecular distance changes occurring during conformational rearrangements within folding MreB bound to chaperonins. We observed that the MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC, indicating that the mechanism of chaperonins is conserved during evolution. The chaperonin-bound MreB is also significantly compacted after addition of AMP-PNP for both the GroEL/ES and TRiC systems. Most importantly, our results showed that GroES may act as an unfoldase by inducing a dramatic initial expansion of MreB (even more than for GroEL) implicating a role for MreB folding, allowing us to suggest a delivery mechanism for GroES to GroEL in prokaryotes.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2016
National Category
Biophysics
Identifiers
urn:nbn:se:liu:diva-130280 (URN)10.1038/srep28386 (DOI)000378228700001 ()27328749 (PubMedID)
Note

Funding Agencies|European Commission [FP7-ICT-2011-7, ERC StG 278242]; Goran Gustafsson Foundation; Swedish Alzheimer Foundation

Available from: 2016-08-01 Created: 2016-07-28 Last updated: 2018-04-25
Hennig, J., Andrésen, C., Museth, A. K., Lundström, P., Tibell, L. & Jonsson, B.-H. (2015). Local Destabilization of the Metal-Binding Region in Human Copper-Zinc Superoxide Dismutase by Remote Mutations Is a Possible Determinant for Progression of ALS. Biochemistry, 54(2), 323-333
Open this publication in new window or tab >>Local Destabilization of the Metal-Binding Region in Human Copper-Zinc Superoxide Dismutase by Remote Mutations Is a Possible Determinant for Progression of ALS
Show others...
2015 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 54, no 2, p. 323-333Article in journal (Refereed) Published
Abstract [en]

More than 100 distinct mutations in the gene CuZnSOD encoding human copper-zinc superoxide dismutase (CuZnSOD) have been associated with familial amyotrophic lateral sclerosis (fALS), a fatal neuronal disease. Many studies of different mutant proteins have found effects on protein stability, catalytic activity, and metal binding, but without a common pattern. Notably, these studies were often performed under conditions far from physiological. Here, we have used experimental conditions of pH 7 and 37 degrees C and at an ionic strength of 0.2 M to mimic physiological conditions as close as possible in a sample of pure protein. Thus, by using NMR spectroscopy, we have analyzed amide hydrogen exchange of the fALS-associated I113T CuZnSOD variant in its fully metalated state, both at 25 and 37 degrees C, where (15)N relaxation data, as expected, reveals that CuZnSOD I113T exists as a dimer under these conditions. The local dynamics at 82% of all residues have been analyzed in detail. When compared to the wild-type protein, it was found that I113T CuZnSOD is particularly destabilized locally at the ion binding sites of loop 4, the zinc binding loop, which results in frequent exposure of the aggregation prone outer beta-strands I and VI of the beta-barrel, possibly enabling fibril or aggregate formation. A similar study (Museth, A. K., et al. (2009) Biochemistry, 48, 8817-8829) of amide hydrogen exchange at pH 7 and 25 degrees C on the G93A variant also revealed a selective destabilization of the zinc binding loop. Thus, a possible scenario in ALS is that elevated local dynamics at the metal binding region can result in toxic species from formation of new interactions at local beta-strands.

Place, publisher, year, edition, pages
American Chemical Society, 2015
National Category
Biological Sciences Chemical Sciences Electrical Engineering, Electronic Engineering, Information Engineering
Identifiers
urn:nbn:se:liu:diva-114994 (URN)10.1021/bi500606j (DOI)000348333300022 ()25496420 (PubMedID)
Note

Funding Agencies|Swedish Research Council [Dnr 2006-4253, Dnr 621-2012-5136]

Available from: 2015-03-09 Created: 2015-03-06 Last updated: 2017-12-04
Babu Moparthi, S., Sjölander, D., Villebeck, L., Jonsson, B.-H., Hammarström, P. & Carlsson, U. (2014). Transient conformational remodeling of folding proteins by GroES - Individually and in concert with GroEL. Journal of chemical biology, 7(1), 1-15
Open this publication in new window or tab >>Transient conformational remodeling of folding proteins by GroES - Individually and in concert with GroEL
Show others...
2014 (English)In: Journal of chemical biology, ISSN 1864-6158, E-ISSN 1864-6166, Vol. 7, no 1, p. 1-15Article, review/survey (Refereed) Published
Abstract [en]

The commonly accepted dogma of the bacterial GroE chaperonin system entails protein folding mediated by cycles of several ATP-dependent sequential steps where GroEL interacts with the folding client protein. In contrast, we herein report GroES-mediated dynamic remodeling (expansion and compression) of two different protein substrates during folding: the endogenous substrate MreB and carbonic anhydrase (HCAII), a well-characterized protein folding model. GroES was also found to influence GroEL binding induced unfolding and compression of the client protein underlining the synergistic activity of both chaperonins, even in the absence of ATP. This previously unidentified activity by GroES should have important implications for understanding the chaperonin mechanism and cellular stress response. Our findings necessitate a revision of the GroEL/ES mechanism.

Place, publisher, year, edition, pages
Springer Berlin/Heidelberg, 2014
Keywords
Carbonic anhydrase; Chaperone; FRET; Molten globule; MreB; Protein folding
National Category
Chemical Sciences Biological Sciences
Identifiers
urn:nbn:se:liu:diva-110534 (URN)10.1007/s12154-013-0106-5 (DOI)24386013 (PubMedID)2-s2.0-84891782616 (Scopus ID)
Available from: 2014-09-14 Created: 2014-09-12 Last updated: 2018-04-25
Ahlner, A., Carlsson, M., Jonsson, B.-H. & Lundström, P. (2013). PINT: a software for integration of peak volumes and extraction of relaxation rates. Journal of Biomolecular NMR, 56(3), 191-202
Open this publication in new window or tab >>PINT: a software for integration of peak volumes and extraction of relaxation rates
2013 (English)In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 56, no 3, p. 191-202Article in journal (Refereed) Published
Abstract [en]

We present the software Peak INTegration (PINT), designed to perform integration of peaks in NMR spectra. The program is very simple to run, yet powerful enough to handle complicated spectra. Peaks are integrated by fitting predefined line shapes to experimental data and the fitting can be customized to deal with, for instance, heavily overlapped peaks. The results can be inspected visually, which facilitates systematic optimization of the line shape fitting. Finally, integrated peak volumes can be used to extract parameters such as relaxation rates and information about low populated states. The utility of PINT is demonstrated by applications to the 59 residue SH3 domain of the yeast protein Abp1p and the 289 residue kinase domain of murine EphB2.

Place, publisher, year, edition, pages
Springer Verlag (Germany), 2013
Keywords
Peak integration, Overlapped peaks, Relaxation rates, Protein dynamics
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-95951 (URN)10.1007/s10858-013-9737-7 (DOI)000321544600001 ()
Note

Funding Agencies|Swedish Research Council||

Available from: 2013-08-19 Created: 2013-08-12 Last updated: 2018-01-11Bibliographically approved
Tegler, L. T., Fromell, K., Jonsson, B.-H., Viljanen, J., Winander, C., Carlsson, J. & Baltzer, L. (2011). Polypeptide Conjugate Binders that Discriminate between Two Isoforms of Human Carbonic Anhydrase in Human Blood.. ChemBioChem (Print), 12(4), 559-566
Open this publication in new window or tab >>Polypeptide Conjugate Binders that Discriminate between Two Isoforms of Human Carbonic Anhydrase in Human Blood.
Show others...
2011 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 12, no 4, p. 559-566Article in journal (Refereed) Published
Abstract [en]

Two binder candidates 4-C37L34-B and 3-C15L8-B from a 16-membered set of 42-residue polypeptide conjugates designed to bind human carbonic anhydrase II (HCAII), were shown to bind HCAII with high affinity in a fluorescence-based screening assay. Two carbonic anhydrase isoforms with 60 % homology exist in human blood with HCAI being present in five- to sevenfold excess over HCAII. The ability of the binders to discriminate between HCAI and HCAII was evaluated with regard to what selectivity could be achieved by the conjugation of polypeptides from a 16-membered set to a small organic molecule that binds both isoforms with similar affinities. The polypeptide conjugate 4-C37L34-B bound HCAII with a K(D) of 17 nM and HCAI with a K(D) of 470 nM, that is, with a 30-fold difference in affinity. The corresponding dissociation constants for the complexes formed from 3-C15L8-B and the two carbonic anhydrases were 60 and 390 nM, respectively. This demonstration of selectivity between two very similar proteins is striking in view of the fact that the molecular weight of each one of the conjugate molecules is little more than 5000, the fold is unordered, and the polypeptide sequences were designed de novo and have no prior relationship to carbonic anhydrases. The results suggest that synthetic polypeptide conjugates can be prepared from organic molecules that are considered to be weak binders with low selectivity, yielding conjugates with properties that make them attractive alternatives to biologically generated binders in biotechnology and biomedicine.

Place, publisher, year, edition, pages
Wiley, 2011
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-65765 (URN)10.1002/cbic.201000556 (DOI)000288080700010 ()21264993 (PubMedID)
Available from: 2011-02-20 Created: 2011-02-20 Last updated: 2017-12-11
Olausson, J., Jonsson, B.-H., Tibell, L. & Påhlsson, P. (2011). Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. Glycobiology, 21(1), 34-44
Open this publication in new window or tab >>Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin
2011 (English)In: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 21, no 1, p. 34-44Article in journal (Refereed) Published
Abstract [en]

Lectins have been widely used in structural and functional studies of complex carbohydrates. Lectins usually bind carbohydrates with relatively low affinity but compensate for this by multivalency. When using lectins in different biological and analytical assays the multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins. The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. It is composed of two identical subunits where each subunit contains five binding sites for fucose. In the present study two forms of recombinant AAL were produced using site-directed mutagenesis. A monomeric form of AAL was produced by exchange of Tyr6 to Arg6, and a monovalent fragment of AAL was produced by insertion of a NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. The AAL forms were expressed as His-tagged proteins in E.coli and purified by affinity chromatography. Binding properties of the two AAL forms were performed using hemagglutination assay, surface plasmon resonance and enzyme-linked lectin assay analyses. Both the monomeric AAL form (mAAL) and the monovalent AAL form (S2-AAL) retained their capacity to bind fucosylated oligosaccharides. However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). Monomeric AAL showed similar binding affinities to fucosylated oligosaccharides compared to rAAL but had less hemagglutinating capacity. S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides such as sialyl-Lex. The study shows that molecular engineering techniques may be a tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. This may be very valuable for development of reliable diagnostic and biological assays for carbohydrate analysis.

Place, publisher, year, edition, pages
Oxford University Press, 2011
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-20310 (URN)10.1093/glycob/cwq129 (DOI)000285193100005 ()
Available from: 2009-09-03 Created: 2009-09-03 Last updated: 2017-12-13
Basaiawmoit, R. V., Oliveira, C. L., Runager, K., Sorensen, C. S., Behrens, M. A., Jonsson, B.-H., . . . Otzen, D. E. (2011). SAXS Models of TGFBIp Reveal a Trimeric Structure and Show That the Overall Shape Is Not Affected by the Arg124His Mutation. JOURNAL OF MOLECULAR BIOLOGY, 408(3), 503-513
Open this publication in new window or tab >>SAXS Models of TGFBIp Reveal a Trimeric Structure and Show That the Overall Shape Is Not Affected by the Arg124His Mutation
Show others...
2011 (English)In: JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, Vol. 408, no 3, p. 503-513Article in journal (Refereed) Published
Abstract [en]

Human transforming growth factor beta induced protein (TGFBIp) is composed of 683 residues, including an N-terminal cysteine-rich (EMI) domain, four homologous fasciclin domains, and an Arg-Gly-Asp (RGD) motif near the C-terminus. The protein is of interest because mutations in the TGFBI gene encoding TGFBIp lead to corneal dystrophy (CD), a condition where protein aggregates within the cornea compromise transparency. The complete three-dimensional structure of TGFBIp is not yet available, with the exception of a partial X-ray structure of the archetype FAS1 domain derived from Drosophila fasciclin-1. In this study, small-angle X-ray scattering (SAXS) models of intact wild-type (WT) human TGFBIp and a mutant (R124H) are presented. The mutation R124H leads to a variant of granular CD. The deduced structure of the TGFBIp monomer consists of four FAS1 domains in a simple "beads-on-a-string" arrangement, constructed by the superimposition of four consecutive Drosophila fasciclin domains. The SAXS-based model of the TGFBIp R124H mutant displayed no structural differences from WT. Both WT TGFBIp and the R124H mutant formed trimers at higher protein concentrations. The similar association properties and three-dimensional shape of the two proteins suggest that the mutation does not induce any major structural rearrangements, but points towards the role of other corneal-specific factors in the formation of corneal R124H deposits.

Place, publisher, year, edition, pages
Elsevier Science B.V., Amsterdam, 2011
Keywords
oligomerization, low-resolution structure, corneal dystrophy, ab initio modeling, rigid-body fit
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-68218 (URN)10.1016/j.jmb.2011.02.052 (DOI)000290067400010 ()
Available from: 2011-05-13 Created: 2011-05-13 Last updated: 2011-05-13
Nygren, P., Lundqvist, M., Liedberg, B., Broo, K., Jonsson, B.-H. & Ederth, T. (2011). Secondary structure in de novo designed peptides induced by electrostatic interaction with particles and membranes.. In: : . Paper presented at Workshop BILL2011 - Bilayers at the Institut Laue Langevin (ILL), Grenoble, France, January 12th - 14th 2011.
Open this publication in new window or tab >>Secondary structure in de novo designed peptides induced by electrostatic interaction with particles and membranes.
Show others...
2011 (English)Conference paper, Poster (with or without abstract) (Other academic)
National Category
Physical Sciences
Identifiers
urn:nbn:se:liu:diva-122696 (URN)
Conference
Workshop BILL2011 - Bilayers at the Institut Laue Langevin (ILL), Grenoble, France, January 12th - 14th 2011
Available from: 2015-11-16 Created: 2015-11-16 Last updated: 2017-01-11Bibliographically approved
Kanmert, D., Brorsson, A.-C., Jonsson, B.-H. & Enander, K. (2011). Thermal Induction of an Alternatively Folded State in Human IgG-Fc. Biochemistry, 50(6), 981-988
Open this publication in new window or tab >>Thermal Induction of an Alternatively Folded State in Human IgG-Fc
2011 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 50, no 6, p. 981-988Article in journal (Refereed) Published
Abstract [en]

We report the formation of a non-native, folded state of human IgG4-Fc induced by a high temperature at neutral pH and at a physiological salt concentration. This structure is similar to the molten globule state in that it displays a high degree of secondary structure content and surface-exposed hydrophobic residues. However, it is highly resistant to chemical denaturation. The thermally induced state of human IgG4-Fc is thus associated with typical properties of the so-called alternatively folded state previously described for murine IgG, IgG-Fab, and individual antibody domains (V(L), V(H), C(H)1, and C(H)3) under acidic conditions in the presence of anions. Like some of these molecules, human IgG4-Fc in its alternative fold exists as a mixture of different oligomeric structures, dominated by an equilibrium between monomeric and heptameric species. Heating further induces the formation of fibrous structures in the micrometer range.

Place, publisher, year, edition, pages
American Chemical Society, 2011
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-65532 (URN)10.1021/bi101549n (DOI)000287049500008 ()21261247 (PubMedID)
Available from: 2011-02-10 Created: 2011-02-10 Last updated: 2017-12-11Bibliographically approved
Owenius, R., Jarl, A., Jonsson, B.-H., Carlsson, U. & Hammarström, P. (2010). GroEL-induced topological dislocation of a substrate protein β-sheet core: a solution EPR spin–spin distance study. Journal of chemical biology, 3(3), 127-39
Open this publication in new window or tab >>GroEL-induced topological dislocation of a substrate protein β-sheet core: a solution EPR spin–spin distance study
Show others...
2010 (English)In: Journal of chemical biology, ISSN 1864-6158, E-ISSN 1864-6166, Vol. 3, no 3, p. 127-39Article in journal (Refereed) Published
Abstract [en]

The Hsp60-type chaperonin GroEL assists in the folding of the enzyme human carbonic anhydrase II (HCA II) and protects it from aggregation. This study was aimed to monitor conformational rearrangement of the substrate protein during the initial GroEL capture (in the absence of ATP) of the thermally unfolded HCA II molten-globule. Single- and double-cysteine mutants were specifically spin-labeled at a topological breakpoint in the β-sheet rich core of HCA II, where the dominating antiparallel β-sheet is broken and β-strands 6 and 7 are parallel. Electron paramagnetic resonance (EPR) was used to monitor the GroEL-induced structural changes in this region of HCA II during thermal denaturation. Both qualitative analysis of the EPR spectra and refined inter-residue distance calculations based on magnetic dipolar interaction show that the spin-labeled positions F147C and K213C are in proximity in the native state of HCA II at 20 °C (as close as ∼8 Å), and that this local structure is virtually intact in the thermally induced molten-globule state that binds to GroEL. In the absence of GroEL, the molten globule of HCA II irreversibly aggregates. In contrast, a substantial increase in spin–spin distance (up to >20 Å) was observed within minutes, upon interaction with GroEL (at 50 and 60 °C), which demonstrates a GroEL-induced conformational change in HCA II. The GroEL binding-induced disentanglement of the substrate protein core at the topological break-point is likely a key event for rearrangement of this potent aggregation initiation site, and hence, this conformational change averts HCA II misfolding.

National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-100534 (URN)10.1007/s12154-010-0038-2 (DOI)21479077 (PubMedID)
Note

At the time of the licentiate theses defence this article was submitted.

Available from: 2013-11-08 Created: 2013-11-08 Last updated: 2018-04-25
Organisations

Search in DiVA

Show all publications