Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Sigrídur H. Thorbjarnardóttir"'
Autor:
Gudmundur O. Hreggvidsson, Jakob K. Kristjansson, Gudmundur Eggertsson, Sigrídur H. Thorbjarnardóttir, Thorarinn Blondal, Snaedis H. Bjornsdottir, Solveig K. Petursdottir, Sigridur Hjorleifsdottir
Publikováno v:
Extremophiles. 10:1-16
Rhodothermus marinus has been the subject of many studies in recent years. It is a thermohalophilic bacterium and is the only validly described species in the genus Rhodothermus. It is not closely related to other well-known thermophiles and is the o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::467462c2918d5c1af11a119b278e8f68
https://doi.org/10.1007/s00792-005-0466-z
https://doi.org/10.1007/s00792-005-0466-z
Autor:
Snaedis H. Bjornsdottir, Sveinn Ernstsson, Astridur Palsdottir, Zophonías O. Jónsson, Sigrídur H. Thorbjarnardóttir, Gudmundur Eggertsson
Publikováno v:
Plasmid. 49:188-191
Here we report the identification and nucleotide sequence analysis of pRM21, a plasmid isolated from the thermophilic eubacterium Rhodothermus marinus. pRM21 consists of 2935 bp, has a G + C content of 58.2% and one major open reading frame whose ded
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c682cb8892abc5da9494da3515e772a0
https://doi.org/10.1016/s0147-619x(02)00152-x
https://doi.org/10.1016/s0147-619x(02)00152-x
Autor:
Sigrídur H. Thorbjarnardóttir, Gudmundur Eggertsson, Magnús M. Kristjánsson, Olafur T. Magnusson, Jóhanna Arnórsdóttir, Rúna B. Smáradóttir
Publikováno v:
European Journal of Biochemistry. 269:5536-5546
The gene encoding a subtilisin-like serine proteinase in the psychrotrophic Vibrio sp. PA44 has been successfully cloned, sequenced and expressed in Escherichia coli. The gene is 1593 basepairs and encodes a precursor protein of 530 amino acid residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4055f05fb9c0dba1fcb3be8507db4531
https://doi.org/10.1046/j.1432-1033.2002.03259.x
https://doi.org/10.1046/j.1432-1033.2002.03259.x
Autor:
Gudmundur Eggertsson, Sunna Helgadóttir, Magnús M. Kristjánsson, Sigrídur H. Thorbjarnardóttir, Jóhanna Arnórsdóttir
Publikováno v:
Biochimica et biophysica acta. 1774(6)
A subtilisin-like serine proteinase from a psychrotrophic Vibrio species (VPR) shows distinct cold adapted traits regarding stability and catalytic properties, while sharing high sequence homology with enzymes adapted to higher temperatures. Based on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b94110844315a3482e1cba92081b012
https://pubmed.ncbi.nlm.nih.gov/17490920
https://pubmed.ncbi.nlm.nih.gov/17490920
Publikováno v:
Applied microbiology and biotechnology. 66(6)
Genetic manipulation of Rhodothermus marinus has been hampered by the lack of a selection system for gene transfer. We report construction of a Rhodothermus/Escherichia coli shuttle plasmid, containing the R. marinus trpB gene, based on pUC18 and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a371ef2f87fbf5cd4199f4a0d309fc9
https://pubmed.ncbi.nlm.nih.gov/15351918
https://pubmed.ncbi.nlm.nih.gov/15351918
Autor:
Jóhanna, Arnórsdottir, Rúna B, Smáradóttir, Olafur Th, Magnússon, Sigrídur H, Thorbjarnardóttir, Gudmundur, Eggertsson, Magnús M, Kristjánsson
Publikováno v:
European journal of biochemistry. 269(22)
The gene encoding a subtilisin-like serine proteinase in the psychrotrophic Vibrio sp. PA44 has been successfully cloned, sequenced and expressed in Escherichia coli. The gene is 1593 basepairs and encodes a precursor protein of 530 amino acid residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a37a43b5e1bf662ba12e9f27dc75ea10
https://pubmed.ncbi.nlm.nih.gov/12423352
https://pubmed.ncbi.nlm.nih.gov/12423352
Autor:
Jón M. Einarsson, Gudmundur Eggertsson, Jakob K. Kristjansson, Sigrídur H. Thorbjarnardóttir, Thorarinn Blondal, Sigridur Hjorleifsdottir, Jan Kieleczawa
Publikováno v:
Biotechnology and applied biochemistry. 34(1)
A gene encoding a DNA polymerase I from the thermophilic eubacterium Rhodothermus marinus was identified. The gene was cloned, sequenced and expressed in Escherichia coli. The gene is 2772 bp long and encodes a protein of 924 amino acids with a calcu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44548a9c37f29a4be04b3db533f2a83b
https://pubmed.ncbi.nlm.nih.gov/11483153
https://pubmed.ncbi.nlm.nih.gov/11483153
Publikováno v:
Nucleic acids research. 28(3)
We describe the characterisation of four thermo-stable NAD(+)-dependent DNA ligases, from Thermus thermophilus (Tth), Thermus scotoductus (Ts), Rhodothermus marinus (Rm) and Thermus aquaticus (Taq), by an assay which measures ligation rate and mismat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5b4f7ce044d5980e2beed177fcca18a
https://pubmed.ncbi.nlm.nih.gov/10637340
https://pubmed.ncbi.nlm.nih.gov/10637340
Autor:
Jakob K. Kristjansson, Jan Kieleczawa, Sigrídur H. Thorbjarnardóttir, Thorarinn Blondal, Jón M. Einarsson, Gudmundur Eggertsson, Sigridur Hjorleifsdottir
Publikováno v:
FEMS microbiology letters. 179(2)
Thymidine kinase type II is an important part of the pyrimidine salvage pathway. The thymidine kinase gene from the thermophilic eubacterium Rhodothermus marinus was cloned, sequenced and overexpressed. The gene is 639 bp and encodes a protein of 213
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::043f03f893ef4862747ee173a4c69857
https://pubmed.ncbi.nlm.nih.gov/10518731
https://pubmed.ncbi.nlm.nih.gov/10518731
Autor:
Olle Holst, Gudmundur Eggertsson, Rémi Spilliaert, Astridur Palsdottir, Jakob K. Kristjansson, Sigrídur H. Thorbjarnardóttir, Gudmundur O. Hreggvidsson, M. Johansson, S. Halldórsdóttir, E. T. Thórólfsdóttir
Publikováno v:
Applied microbiology and biotechnology. 49(3)
A gene library from the thermophilic eubacterium Rhodothermus marinus, strain ITI 378, was constructed in pUC18 and transformed into Escherichia coli. Of 5400 transformants, 3 were active on carboxymethylcellulose. Three plasmids conferring cellulase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::576b4f690c2f52e322d080221306102f
https://pubmed.ncbi.nlm.nih.gov/9581291
https://pubmed.ncbi.nlm.nih.gov/9581291