Zobrazeno 1 - 10
of 12
pro vyhledávání: '"J. M. van Dijl"'
Autor:
J. W. A. Schoenmakers, R. de Boer, L. Gard, G. A. Kampinga, M. van Oosten, J. M. van Dijl, P. C. Jutte, M. Wouthuyzen-Bakker
Publikováno v:
Journal of Bone and Joint Infection, Vol 8, Pp 45-50 (2023)
Background: prompt recognition and identification of the causative microorganism in acute septic arthritis of native and prosthetic joints is vital to increase the chances of successful treatment. The aim of this study was to independently assess the
Externí odkaz:
https://doaj.org/article/d8888928be8740728b591515293734cc
Publikováno v:
Molecular and General Genetics MGG. 254:81-84
A mutation leading to roseoflavin resistance and deregulated riboflavin biosynthesis was mapped in the genome of the riboflavin-overproducing Bacillus subtilis strains RB52 and RB50 at map position 147 degrees. The chromosomal location indicates that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82f584e9127824436a909a913d89b867
https://doi.org/10.1007/s004380050393
https://doi.org/10.1007/s004380050393
Publikováno v:
Molecular and General Genetics, 223(2), 233-240
A system is described which enabled the selection of a heterologous lep gene, encoding signal peptidase I, in Escherichia coli. It is based on complementation of an E. coli mutant, in which the synthesis of signal peptidase I can be regulated. With t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d59cb2d8147f6121026e0e07b01f0d5
https://doi.org/10.1007/bf00265059
https://doi.org/10.1007/bf00265059
Autor:
H L, Hyyryläinen, A, Bolhuis, E, Darmon, L, Muukkonen, P, Koski, M, Vitikainen, M, Sarvas, Z, Prágai, S, Bron, J M, van Dijl, V P, Kontinen
Publikováno v:
Molecular microbiology. 41(5)
The Gram-positive eubacterium Bacillus subtilis is well known for its high capacity to secrete proteins into the environment. Even though high-level secretion of proteins is an efficient process, it imposes stress on the cell. The present studies wer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eae6ebf7bbbe37b0d25ed194693d96db
https://pubmed.ncbi.nlm.nih.gov/11555295
https://pubmed.ncbi.nlm.nih.gov/11555295
Autor:
H, Tjalsma, V P, Kontinen, Z, Prágai, H, Wu, R, Meima, G, Venema, S, Bron, M, Sarvas, J M, van Dijl
Publikováno v:
The Journal of biological chemistry. 274(3)
Computer-assisted analyses indicate that Bacillus subtilis contains approximately 300 genes for exported proteins with an amino-terminal signal peptide. About 114 of these are lipoproteins, which are retained in the cytoplasmic membrane. We have inve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4381082bee40090a3b1708566aaecd39
https://pubmed.ncbi.nlm.nih.gov/9880550
https://pubmed.ncbi.nlm.nih.gov/9880550
Publikováno v:
The Journal of biological chemistry. 272(41)
Most biological membranes contain one or two type I signal peptidases for the removal of signal peptides from secretory precursor proteins. In this respect, the Gram-positive bacterium Bacillus subtilis seems to be exceptional, because it contains at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6f0c55e29e9bce0ab1115653288bbbc1
https://pubmed.ncbi.nlm.nih.gov/9325333
https://pubmed.ncbi.nlm.nih.gov/9325333
Publikováno v:
Protein science : a publication of the Protein Society. 6(6)
The discovery that proteins exported from the cytoplasm are typically synthesized as larger precursors with cleavable signal peptides has focused interest on the peptidases that remove the signal peptides. Here, we review the membrane-bound peptidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::59db8451d55af7d28507326b1faac696
https://pubmed.ncbi.nlm.nih.gov/9194173
https://pubmed.ncbi.nlm.nih.gov/9194173
Publikováno v:
The Journal of biological chemistry. 270(8)
Signal peptidases remove signal peptides from secretory proteins. By comparing the type I signal peptidase, SipS, of Bacillus subtilis with signal peptidases from prokaryotes, mitochondria, and the endoplasmic reticular membrane, patterns of conserve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::36179a3526d56a995419998784ba45d3
https://pubmed.ncbi.nlm.nih.gov/7876097
https://pubmed.ncbi.nlm.nih.gov/7876097
Publikováno v:
FEMS microbiology letters. 65(3)
This paper describes an attempt to clone the Bacillus licheniformis lep gene, encoding signal peptidase, using the Salmonella typhimurium lep gene as a hybridization probe. Although a hybridizing fragment was obtained, DNA sequence analysis indicated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5426e9222343e178e64c179fb9d1db60
https://pubmed.ncbi.nlm.nih.gov/1916233
https://pubmed.ncbi.nlm.nih.gov/1916233
Previously, curing experiments suggested that plasmid pWV05 (17.5 megadaltons [Md]) of Streptococcus cremoris Wg2 specifies proteolytic activity. A restriction enzyme map of pWV05 was constructed, the entire plasmid was subcloned in Escherichia coli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2477e9e5bff25709802cd4906344f31
https://europepmc.org/articles/PMC238578/
https://europepmc.org/articles/PMC238578/
