| 1. |
- Johansson, Tomas, et al.
(författare)
-
The gene from the white-rot fungus Trametes versicolor encoding the lignin peroxidase isozyme LP7*1
- 1995
-
Ingår i: Biochimica et Biophysica Acta, Gene Structure and Expression. - 0167-4781. ; 1263:1, s. 71-74
-
Tidskriftsartikel (refereegranskat)abstract
- The structural gene LPGVI (1463 bp including 6 introns), characterized from the white-rot basidiomycete Trametes versicolor (PRL 572), encodes a 342-residue mature polypeptide of 36.7 kDa, preceded by a 26-residue signal/propeptide. LPGVI is identified as the gene encoding the 43 kDa lignin peroxidase isozyme LP7 as based on the partial amino acid sequence information available. The polypeptide deduced shares 72–74% identity in sequence with other lignin peroxidases and 70% with a manganese (II) peroxidase from T. versicolor.
|
|
| 2. |
- Karlsson, Eva Nordberg, et al.
(författare)
-
Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus
- 1997
-
Ingår i: Biochimica et Biophysica Acta - Gene Structure and Expression. - 0167-4781. ; 1353:2, s. 118-124
-
Tidskriftsartikel (refereegranskat)abstract
- The gene (xyn1) encoding a Rhodothermus marinus xylanase has been cloned and expressed in Escherichia coli. The gene comprises 5 different domains in an unusual combination. The cellulose binding domains (CBDs) encoded by xyn1 are repeated in tandem at the N-terminus and show similarity with the CBD family IV. The xyn1-gene is the first example encoding a CBD family IV in combination with a xylan hydrolyzing catalytic domain of the glycosyl hydrolase family 10.
|
|
| 3. |
- Kim, S. K., et al.
(författare)
-
Binding of RecA to anti-parallel poly(dA) · 2poly(dT) triple helix DNA
- 1995
-
Ingår i: Biochimica et Biophysica Acta - Gene Structure and Expression. - : Elsevier BV. - 0167-4781. ; 1264:1, s. 129-133
-
Tidskriftsartikel (refereegranskat)abstract
- Binding of RecA protein to conventional anti-parallel poly(dA). 2poly(dT) tripler DNA has been studied using flow linear dichroism spectroscopy. The association requires the presence of cofactor analog adenosine 5'-O-3-thiotriphosphate (ATP gamma S) and occurs with a rate similar to that for the association of RecA to double-stranded poly(dA) poly(dT) DNA. The binding of RecA to DNA stiffens the nucleotide chain, as evidenced from high orientation already at low shear rates, and the complex with tripler DNA appears to be at least as stiff as that with the duplex DNA. Therefore, the observation of a lower magnitude of the LD spectrum at 260 nm, in the triplex-RecA compared to the duplex-RecA complex, but retained magnitude of protein LD at 280 nm, indicates a markedly impaired orientation of nucleo-bases, possibly reflecting a perturbation by RecA on the third strand making its bases deviate strongly from perpendicularity. The circular dichroism spectrum: appearing immediately after dissociation of RecA by SDS, suggests an intact tripler structure, meaning that complexation with RecA has not dissociated the third strand. In conclusion, binding of RecA to tripler DNA does not modify the main organisation of the strands, but could affect the base-base interactions between them. Tilted bases could reflect a conformational change that RecA imposes also on the biological intermediate tripler structure to relax the base-base hydrogen bonding between the DNA strands.
|
|
| 4. |
- Lindqvist, A, et al.
(författare)
-
Bovine alpha 1-microglobulin/bikunin. Isolation and characterization of liver cDNA and urinary alpha 1-microglobulin
- 1996
-
Ingår i: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002. ; 1306:1, s. 98-106
-
Tidskriftsartikel (refereegranskat)abstract
- cDNA coding for alpha 1-microglobulin, an immunoregulatory plasmaprotein, was isolated from bovine liver. The sequence of a total of 1258 nucleotides revealed an open reading frame of 352 amino acids. This included alpha 1-microglobulin, 182 amino acids, and bikunin, the light chain of the plasmaprotein inter-alpha-inhibitor, 147 amino acids. The two proteins were connected by a basic tetrapeptide, R-A-R-R, which conforms to the consensus sequence recognized by endoproteolytic cleavage enzymes. The deduced amino acid sequence showed a high degree of identity with alpha 1-microglobulin and bikunin sequences from other species, and the alpha 1-microglobulin part displayed sequence motifs typical for members of the lipocalin protein superfamily. A single alpha 1-microglobulin/bikunin mRNA with a size of around 1300 nt was found in bovine liver. The mature alpha 1-microglobulin protein was isolated from bovine urine, and partly characterized. It was found to be a globular molecule with an apparent molecular weight of 23,300, containing one N-linked and at least on O-linked oligosaccharide, one intra-chain disulfide bridge and an electrophoretic heterogeniety with a pI-value of 4.1-5.2.
|
|
| 5. |
- Lindqvist, A, et al.
(författare)
-
Rat alpha 1-microglobulin : co-expression in liver with the light chain of inter-alpha-trypsin inhibitor
- 1992
-
Ingår i: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002. ; 1130:1, s. 7-63
-
Tidskriftsartikel (refereegranskat)abstract
- A 1162 bp rat liver cDNA clone encoding the immunoregulatory plasma protein alpha 1-microglobulin was isolated and sequenced. The open reading frame encoded a 349 amino acid polyprotein, including alpha 1-microglobulin, 182 amino acids, and bikunin, the light chain of the plasma protein inter-alpha-trypsin inhibitor, 145 amino acids. The alpha 1-microglobulin/bikunin mRNA was found only in the liver when different tissues were examined. Free alpha 1-microglobulin and a polyprotein, containing both alpha 1-microglobulin and inter-alpha-trypsin inhibitor epitopes, were found in the microsomal fraction from rat liver homogenates.
|
|
| 6. |
- Behravan, Gity, et al.
(författare)
-
Formation of a free radical of the sulfenylimine type in the mouse ribonucleotide reductase reaction with 2'-azido-2'-deoxycytidine 5'-diphosphate
- 1995
-
Ingår i: Biochimica et Biophysica Acta, Gene Structure and Expression. - : Elsevier BV. - 0167-4781 .- 1879-2634. ; 1264:3, s. 323-329
-
Tidskriftsartikel (refereegranskat)abstract
- Mouse and Escherichia coli ribonucleotide reductases (RR) both belong to the same class of RR, where the enzyme consists of two non-identical subunits, proteins R1 and R2. A transient free radical was observed by EPR spectroscopy in the mouse RR reaction with the suicidal inhibitor 2′-azido-2′-deoxycytidine 5′-diphosphate. The detailed hyperfine structure of the EPR spectrum of the transient radical is somewhat different for the mouse and previously studied E. coli enzymes. When the positive allosteric effector ATP was replaced by the negative effector dATP, no transient radical was observed, showing that ‘normal' binding of the inhibitor to the substrate binding site is required. Using the mouse protein R2 mutants W 103Y and D266A, where the mutations have been shown to specifically block long range electron transfer between the active site of the R1 protein to the iron/radical site in protein R2, no evidence of transient radical was found. Taken together, the data suggest that the radical is located at the active site in protein R1, and is probably of the sulfenylimine type
|
|
| 7. |
|
|
| 8. |
- Gittins, John R., et al.
(författare)
-
Identification of a novel nuclear factor-binding site in the Pisum sativum sad gene promoters
- 2002
-
Ingår i: Biochimica et Biophysica Acta, Gene Structure and Expression. - 0167-4781 .- 1879-2634. ; 1574:3, s. 231-244
-
Tidskriftsartikel (refereegranskat)abstract
- DNA fragments containing the 5' promoter regions of the Pisum sativum sadA and sadC genes were amplified from genomic DNA, cloned and sequenced. These sequences contain a number of conserved cis-acting elements, which are potentially involved in stress-induced transcription of the sad genes. To determine whether any of the identified elements are active in binding nuclear factors in vitro, 11 60-bp overlapping (by 30 bp) DNA probe fragments covering the proximal sadC promoter sequence (360 bp) were used in electrophoretic mobility shift assays with competition. Binding activities were compared in nuclear extracts from control, UV-B-stressed and wounded pea leaves. The pattern of DNA binding was almost identical with all three extracts, with one 30-bp region being the predominant site for factor binding. Using overlapping sub-fragments of this region, the majority of the specific binding could be attributed to the novel 11-bp GC-rich sequence GTGGCGCCCAC. An almost identical sequence is conserved in the sadA promoter. This motif has features in common with a number of recognised cis-elements, which suggests a possible binding site for factors which play a role in regulating sad gene transcription.
|
|
| 9. |
- Johansson, H., et al.
(författare)
-
Molecular cloning and characterization of a cDNA encoding poplar UDP-glucose dehydrogenase, a key gene of hemicellulose/pectin formation
- 2002
-
Ingår i: Biochimica et Biophysica Acta, Gene Structure and Expression. - 0167-4781 .- 1879-2634. ; 1576:02-jan, s. 53-58
-
Tidskriftsartikel (refereegranskat)abstract
- Plant UDP-glucose dehydrogenase (UGDH) is an important enzyme in the formation of hemicellulose and pectin, the components of newly formed cell walls. A cDNA clone (Ugdh) corresponding to UGDH was isolated from a cDNA library prepared from cambial zone of poplar (Populus tremula x tremuloides). Within the 1824-nucleotide (nt)-long clone, an open reading frame encoded a protein of 481 amino acids (aa), with a calculated molecular weight of 53.1 kDa. The derived aa sequence showed 90% and 63% identity with UGDHs from soybean and bovine liver, respectively, and had highly conserved aa motifs believed to be of importance for nt binding and catalytic efficiency. In poplar, the Ugdh corresponds to one or two genes, as found by genomic Southern analysis. The gene was expressed predominantly in differentiating xylem and young leaves, with little expression in the phloem zone of the stem. The expression pattern matched that of UGDH protein, as found by immunoblotting. In leaves, the Ugdh expression was upregulated by a short-term feeding with sucrose, sorbitol and polyethylene glycol, and this effect was to some extent mimicked by light exposure. The data suggest that Ugdh is regulated via an osmoticum-dependent pathway, possibly related to the availability of osmotically active carbohydrate precursors to UDPglucose, a substrate of UGDH.
|
|
| 10. |
|
|
