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  • 1
    Electronic Resource
    Electronic Resource
    Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH (1988)
    Springer
    Archives of microbiology 150 (1988), S. 405-412 
    Details
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; Activation ; Corrinoid enzyme ; Methyltransferase ; Methanopterin ; Coenzyme M
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The enzymatic conversion of formaldehyde to CH3S-CoM in crude extracts of Methanobacterium thermoautotrophicum was used as a means to investigate the methyl-tetrahydromethanopterin: HS-CoM methyltransferase reaction. All components necessary for formaldehyde conversion were shown to be present in a soluble protein fraction. This soluble cell fraction still contained a major amount of corrinoids. Apart from tetrahydromethanopterin no other soluble cofactors were required for formaldehyde conversion. The dependence of the system on catalytic amounts of ATP was shown to be specific. Several nucleoside triphosphates or ADP were unable to substitute for ATP. Remarkably, various strong reducing systems, especially titanium(III)citrate could replace ATP to a large extent. The ATP-dependent formaldehyde conversion to CH3S-CoM was inhibited in the presence of nitrous oxide, detergents or 2′,3′-dialdehyde-ATP. The results support a role for a corrinoid protein in the methyl-tetrahydromethanopterin: HS-CoM methyltransferase reaction at which ATP is involved in the activation of this protein, probably in the conversion of inactive B12a or B12r to active B12s.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408315
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  • 2
    Electronic Resource
    Electronic Resource
    In vitro splicing of pre-mRNA containing bromouridine (1994)
    Springer
    Molecular biology reports 19 (1994), S. 109-113 
    Details
    ISSN: 1573-4978
    Keywords: bromouridine ; nucleotide analogue ; pre-mrna ; polypyrimidine tract ; splicing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The artificial UTP-analogue 5-bromouridine 5′-triphosphate (BrUTP) has been used to label pre-mRNAin vitro andin vivo [1, 2]. We have investigated the effect of bromouridine (BrU) in pre-mRNA on the efficiency of splicing. An adenovirus major late II construct was used to prepare four different transcripts, each containing a different amount of BrU. These four transcripts were tested in anin vitro splicing assay. We found that splicing is strongly inhibited if all uridines (U) in the transcript were substituted for BrU. Splicing was restored to some extent if 50% of the Us were replaced by BrU. The splicing efficiency returned to an almost normal level if only I out of every 10 Us was substituted for BrU. This demonstrates that only a pre-mRNA containing a small amount of BrU can be spliced normallyin vitro. Furthermore, these results strongly suggest that some Us in the adenoviral transcript, probably those at the splice sites, cannot be replaced by BrU and are therefore critical in the splicing reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00997156
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    Paper (German National Licenses)
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