| 1. |
- Aevarsson, A, et al.
(author)
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Ligands to the 2Fe iron-sulfur center in succinate dehydrogenase
- 1988
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In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 232:2, s. 298-302
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Journal article (peer-reviewed)abstract
- Membrane-bound succinate oxidoreductases are flavoenzymes containing one each of a 2Fe, a 3Fe and a 4Fe iron-sulfur center. Amino acid sequence homologies indicate that all three centers are located in the Ip (B) subunit. From polypeptide and gene analysis of Bacillus subtillis succinate dehydrogenase-defective mutants combined with earlier EPR spectroscopic data, we show that four conserved cysteine residues in the first half of Ip are the ligands to the [2Fe-2S] center. These four residues have previously been predicted to be the ligands. Our results also suggest that the N-terminal part of B. subtilis Ip constitutes a domain which can incorporate separately the 2Fe center and interact with Fp, the flavin-containing subunit of the dehydrogenase.
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| 2. |
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| 3. |
- Bratt, T, et al.
(author)
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Processing and secretion of rat alpha 1-microglobulin-bikunin expressed in eukaryotic cell lines
- 1994
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In: FEBS Letters. - : Wiley. - 0014-5793. ; 354:1, s. 57-61
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Journal article (peer-reviewed)abstract
- The precursor protein alpha 1-microglobulin-bikunin was cleaved to the same degree whether expressed in CHO cells or in mutated CHO cells, RPE.40 cells, suggested to lack a functional form of the intracellular protease furin. Thus, alpha 1-microglobulin-bikunin probably is not cleaved in vivo by furin. However, simultaneous overexpression of the precursor and furin in COS, CHO and RPE.40 cells increased the cleavage, suggesting that compartmentalisation and concentrations of protease and precursor are important for the cleavage, besides the in vitro specificity. Expression of alpha 1-microglobulin and bikunin alone gave different protein patterns of SDS-PAGE as compared to expression of the precursor and subsequent cleavage, suggesting that the precursor protein is important for the post-translational handling of alpha 1-microglobulin and bikunin.
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| 6. |
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| 7. |
- Hillarp, A, et al.
(author)
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Protein S binding in relation to the subunit composition of human C4b-binding protein
- 1989
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In: FEBS Letters. - : Wiley. - 0014-5793. ; 259:1, s. 6-53
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Journal article (peer-reviewed)abstract
- The human regulatory complement component C4b-binding protein (C4BP) circulates in plasma either as a free protein or in a bimolecular complex with the vitamin K-dependent protein S. The major form of C4BP is composed of 7 identical, disulfide-linked 70 kDa subunits (alpha-chains), the arrangement of which gives the C4BP molecule a spider-like appearance. Recently, we identified a unique 45 kDa subunit (beta-chain) in C4BP. We have now isolated a subpopulation of C4BP, which does not bind protein S. This C4BP species, which had a molecular weight slightly lower than that of the predominant form, was found to lack the beta-chain. Another lower molecular weight form of C4BP was also purified. It contained the beta-chain and was efficient in binding protein S. Its subunit composition was judged to comprise six alpha-chains and one beta-chain. These results indicate C4BP in plasma to be heterogeneous at a molecular level vis-a-vis subunit composition and/or protein S binding ability and provide support for the concept that the beta-chain of C4BP contains the single protein S binding site.
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| 8. |
- Hägerhäll, Cecilia, et al.
(author)
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A structural model for the membrane-integral domain of succinate:quinone oxidoreductases
- 1996
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In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793.
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Journal article (peer-reviewed)abstract
- Many succinate:quinone oxidoreductases in bacteria and mitochondria, i.e, succinate:quinone reductases and fumarate reductases, contain in the membrane anchor a cytochrome b whose structure and function is poorly understood, Based on biochemical data and polypeptide sequence information, we show that the anchors in different organisms are related despite an apparent diversity in polypeptide and heme composition, A general structural model for the membrane-integral domain of the anchors is proposed, It is an antiparallel four-helix bundle with a novel arrangement of hexa-coordinated protoheme M. The structure can be applied to a larger group of membrane-integral cytochromes of b-type and has evolutionary and functional implications.
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| 9. |
- Kim, Seog K., et al.
(author)
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METHYL GREEN - A DNA MAJOR-GROOVE BINDING-DRUG
- 1993
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In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 315:1, s. 61-64
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Journal article (peer-reviewed)abstract
- Interaction and binding geometries of complexes of Methyl green with poly(dA-dT)2, poly(dA) . poly(dT), and triplex poly(dA) . 2poly(dT) complexes have been studied by linear dichroism. For both of the complexes with double helical DNAs, the z symmetry axis of Methyl green is found to be approximately parallel to the DNA bases while the x symmetry axis lies at 40-44-degrees relative to the local DNA helix axis, in agreement with a groove binding mode. However, in contrast to minor-groove binders (such as DAPI and Hoechst 33258) Methyl green is found to be excluded from binding to the triple helical poly(dA) . 2poly(dT) in which the major groove is filled by the third strand. While most so far studied groove-binding dyes bind in the minor groove of DNA, Methyl green thus appears to be an exception.
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| 10. |
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