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  • 1
    Electronic Resource
    Electronic Resource
    A new insertion element, ISH26, from Halobacterium halobium (1987)
    Springer
    Molecular genetics and genomics 206 (1987), S. 81-87 
    Details
    ISSN: 1617-4623
    Keywords: Insertion elements of H. halobium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new halobacterial insertion element, ISH26, is described which occurs in the genome of Halobacterium halobium NRC817 in at least seven copies. A copy of ISH26 was isolated from the bacterio-opsin gene (bop) of the Bop mutant M140 of strain H. halobium R1 and characterized in more detail. It shows typical structural features of a transposable element with 16 pb terminal inverted repeat sequences and an 11 bp duplication of the target site. Two partially overlapping open reading frames (ORFs) are contained in the sequence of ISH26 on one strand. The terminal 16 bp inverted repeat of ISH26 is almost identical to the first 16 bp of the terminal inverted repeat of the ISH2 insertion element. The remaining sequences of ISH26 and ISH2 are entirely different. Two size variants of ISH26, 1,384 bp and 1,705 bp in size, are found in the H. halobium genome. The larger one (ISH26-1) contains an imperfect duplication of 321 bp at one end of ISH26.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326540
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by theEscherichia coli hemolysin transport system (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 42-48 
    Details
    ISSN: 1617-4623
    Keywords: Secretion ; Recombinant DNA ; Hemolysin ; HlyB/H1yD complementation ; OmpT protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A fusion gene (ces-hlyA s) was constructed by ligating the genetic information for the C-terminal 60 amino acids (hlyA s) ofEscherichia coli hemolysin (H1yA) to the ces gene for a cholesterol esterase/lipase (CE) from aPseudomonas species. Part (about 30 %) of the expressed fusion protein CE-H1yAs was secreted inE. coli carryinghlyB andhlyD genes. Following the insertion between the reporter gene andhlyA s of a linker sequence that contains the information for potential cleavage sites for the outer membrane protease OmpT, two different fusion proteins (PhoA-H1yAs and CE-HlyAs) were shown to be cleaved by OmpT between the two parts during H1yB/H1yD-mediated secretion. Processed PhoA and CE accumulated in the supernatant. The efficiency of cleavage by OmpT was considerably improved by increasedompT gene dose. It was further shown that OmpT preferentially recognizes potential cleavage sites within the linker sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00587559
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    Paper (German National Licenses)
    Fulltext
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