Neurospora, primary structure

Metallothioneins from Neurospora crassa contain only 25 amino acid residues, but the primary structure is quite similar to the N-terminal part of the mammalian proteins.1454 These data indicate that the gene that codes for the Neurospora crassa metallothionein is evolutionary related to the gene of the vertebrate metallothioneins. Equine metallothionein exists in two major variants (metallothionein 1A and metallothionein 2A), which show remarkable similarities. Some allelic polymorphic variants also occur in man, horse and rabbit. Recent developments have been comprehensively reviewed.14678... 

Lerch, K. (1982). Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether. J. Biol. Chem., 257, 6414-6419. 

From the primary structures bovine cytochrome c, [181], human [182], bovine [153], mouse [183], Saccharomyces [184], Aspergillus [185], and Neurospora [186] cytochrome b. Studies on the bovine [187] and Neurospora [188,189] Complex III are summarised. Complex III from rat [190] and Saccharomyces [191] are very similar but the latter may lack the smallest subunit , band VIII [192]. The complex forms dimers in Triton X-100 [189,192,193]. 

Molecular studies on various GDH s are now proceeding rapidly since elucidation of the primary structures of some of these enzymes. It is essential to note, however, that these enzymes vary not only in coenzyme specificity but also in other properties, e.g., induction and repression of synthesis by metabolites, regulation of activity by purine nucleoside di-and triphosphates, e.g., ADP, GDP, ATP, GTP, and other ligands, and in molecular properties. The successful isolation from some species of modified forms of the enzyme produced by mutant strains, particularly of Neurospora, now permits identification of residues important for maintenance of normal activity. 

As the prototypic member of microbial RNases, RNase T1 shares a similar catalytic mechanism and varying degrees of primary and, when known, tertiary structural identities with other guanylo-RNases, such as RNase U1 from Ustilago sphaerogena (39), RNase N1 from Neurospora crassa (39), and bamase from Bacillus amyloliquefaciens (48). 

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