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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 22 (1985), S. 20-31 
    ISSN: 1432-1432
    Keywords: Origin of life ; Ancestral sequence ; Sequence homology ; Protein evolution ; Gene duplication ; Gene transposition ; Electron transport proteins ; Fe∶S clusters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Recent evidence indicates that a gene transposition event occurred during the evolution of the bacterial ferredoxins subsequent to the ancestral intrasequence gene duplication. In light of this new information, the relationships among the bacterial ferredoxins were reexamined and an evolutionary tree consistent with this new understanding was derived. The bacterial ferredoxins can be divided into several groups based on their sequence properties; these include the clostridial-type ferredoxins, theAzotobacter-type ferredoxins, and a group containing the ferredoxins from the anaerobic, green, and purple sulfur bacteria. Based on sequence comparison, it was concluded that the amino-terminal domain of theAzotobacter-type ferredoxins, which contains the novel 3Fe∶3S cluster binding site, is homologous with the carboxyl-terminal domain of the ferredoxins from the anaerobic photosynthetic bacteria. A number of ferredoxin sequences do not fit into any of the groups described above. Based on sequence properties, these sequences can be separated into three groups: a group containingMethanosarcina barkeri ferredoxin andDesulfovibrio desulfuricans ferredoxin II, a group containingDesulfovibrio gigas ferredoxin andClostridium thermoaceticum ferredoxin, and a group containingDesulfovibrio africanus ferredoxin I andBacillus stearothermophilus ferredoxin. The last two groups differ from all of the other bacterial ferredoxins in that they bind only one Fe∶S cluster per polypeptide, whereas the others bind two. Sequence examination indicates that the second binding site has been either partially or completely lost from these ferredoxins.Methanosarcina barkeri ferredoxin andDesulfovibrio desulfuricans ferredoxin II are of interest because, of all the ferredoxins whose sequences are presently known, they show the strongest evidence of internal gene duplication. However, the derived evolutionary tree indicates that they diverged from theAzotobacter-type ferredoxins well after the ancestral internal gene duplication. This apparent discrepancy is explained by postulating a duplication of one halfchain sequence and a deletion of the other halfchain. TheClostridium thermoaceticum andBacillus stearothermophilus groups diverged from this line and subsequently lost one of the Fe∶S binding sites. It has recently become apparent that gene duplication is ubiquitous among the ferredoxins. Several organisms are now known to have a variety of ferredoxins with widely divergent properties. Unfortunately, in only one case are the sequences of more than one ferredoxin from the same organism known. Thus, although the major features of the bacterial ferredoxin tree are now understood, a complete bacterial phylogeny cannot be inferred until more sequence information is available.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 21 (1985), S. 126-132 
    ISSN: 1432-1432
    Keywords: Ragweed allergen Ra3 ; Stellacyanin ; Basic blue protein ; Plastocyanin ; Azurin ; Type 1 copper-binding proteins ; Distantly related protein sequences ; Protein superfamily ; Evolutionary tree ; Computer methods
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have found ragweed allergen Ra3 to be related to the type 1 copper proteins; it is most closely related to stellacyanin and basic blue protein. The type 1 copper proteins form a diverse group of proteins, most of which are involved in electron transport. However, key amino acids believed to be involved in copper binding are absent from the allergen sequence; thus, the allergen is not likely to be functionally related to the type 1 copper proteins. We have grouped these proteins into one superfamily and we depict the relationships among them by an evolutionary tree. As indicated by this tree, an ancient gene duplication resulted in the divergence of plastocyanin from the line leading to basic blue protein, stellacyanin, and allergen Ra3.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Origins of life and evolution of the biospheres 12 (1982), S. 311-319 
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR-We have questioned12 the significance of similarities noted by Haseltine and Patarca3 between the scrapie-associa-ted protein, PrP 27-30, and the human immunodeficency virus, HIV-1. Patarca et al.4 defend the significance of this sequence resemblance. This supposed relationship could affect ...
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4943
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The quantification of proteins in silver-stained electrophoresis gels has been limited by the differences in “stainability” of different proteins. Despite efforts by many researchers, the precise basis of the reaction between silver reagents and polypeptides is still unclear, and, depending on the formulation, may even differ. We have tested the hypothesis that differences in stainability among proteins can be attributed to diferences in di- or tripeptide composition. The results indicate that some order of protein structure other than short peptides accounts for the staining differences observed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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