Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

Bruinenberg, P.M.; Evers, Melchior E.; Waterham, Hans R.; Kuipers, Jeroen; Arnberg, Annika C.; Ab, Geert

doi:10.1016/0167-4781(80)90003-2

Cited by 87 publications

(42 citation statements)

References 54 publications

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“…In keeping with these findings, the similarity between S. cerevisiae Prt1p and the putative Prt1p from H. polymorpha (5) begins close to the methionine encoded by the first ATG in the H. polymorpha gene but downstream of the second ATG in the S. cerevisiae gene (Fig. 6A).…”

Section: Discussionsupporting

confidence: 48%

Mutational Analysis of the Prt1 Protein Subunit of Yeast Translation Initiation Factor 3

Evans

Rasmussen

Hanic-Joyce

et al. 1995

Molecular and Cellular Biology

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The Saccharomyces cerevisiae PRT1 gene product Prt1p is a component of translation initiation factor eIF-3, and mutations in PRT1 inhibit translation initiation. We have investigated structural and functional aspects of Prt1p and its gene. Transcript analysis and deletion of the PRT1 5 end revealed that translation of PRT1 mRNA is probably initiated at the second in-frame ATG in the open reading frame. The amino acid changes encoded by six independent temperature-sensitive prt1 mutant alleles were found to be distributed throughout the central and C-terminal regions of Prt1p. The temperature sensitivity of each mutant allele was due to a single missense mutation, except for the prt1-2 allele, in which two missense mutations were required. In-frame deletion of an N-terminal region of Prt1p generated a novel, dominant-negative form of Prt1p that inhibits translation initiation even in the presence of wild-type Prt1p. Subcellular fractionation suggested that the dominant-negative Prt1p competes with wild-type Prt1p for association with a component of large Prt1p complexes and as a result inhibits the binding of wild-type Prt1p to the 40S ribosome.Mutations in the PRT1 gene of the yeast Saccharomyces cerevisiae, as exemplified by the temperature-sensitive prt1-1 mutant allele, cause a conditional impairment of translation initiation in vivo (26, 27; see also reference 18); in vitro, prt1-1 mutant cell extracts are defective for the interaction of the eIF-2 GTP Met-tRNA i ternary complex with the 40S ribosomal subunit (16), suggesting that the PRT1 polypeptide (Prt1p) may be a component of the yeast translation initiation factor 3 (eIF-3) complex (37, 38). Recently, this suggestion has been validated by the identification of Prt1p in purified yeast .Mutant forms of the PRT1 gene have been found several times by selection for temperature-sensitive growth mutants (26,27,58) and also through searches for more-specific effects. The prt1-63 allele (formerly cdc63 [22]) was obtained by selection for mutants conditionally unable to perform the G 1 cell cycle regulatory step (2), whereas the prt1-26 allele (formerly dna26 [15]) was identified in a mutant defective for DNA synthesis (13). The identification of prt1 mutant alleles by the latter criteria can be understood from the effects of prt1 mutations on the cell cycle. At appropriate restrictive temperatures, all temperature-sensitive prt1 mutations can cause regulated cell cycle blockage (23), and the DNA synthesis impairment caused by the prt1-26 mutation was shown to be an indirect consequence of a concerted arrest of mutant cells in the G 1 phase of the cell cycle (15). Thus, prt1 mutant alleles can allow sufficient protein synthesis for completion of an ongoing cell cycle (7) while blocking initiation of the next cell cycle and DNA replication.Prt1p has been characterized by analysis of the cloned PRT1 gene (24). In this report, we extend the characterization of Prt1p by showing that the open reading frame (ORF) of PRT1 does not accurately predict Prt1p and by identi...

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Section: Discussionsupporting

confidence: 48%

Mutational Analysis of the Prt1 Protein Subunit of Yeast Translation Initiation Factor 3

Evans

Rasmussen

Hanic-Joyce

et al. 1995

Molecular and Cellular Biology

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“…Elucidation of the 1,4-diamin0-2-butynebinding site and its consensus sequence is now in progress. When the amino acid sequence near the active site, towards, the amino terminus, was compared for amine oxidases from various sources [23,[26][27][28][29][30][31][32], as shown in Fig. 9, some similarity around the position of the 1,4-diamino-2-butyne-binding site of A. niger AO-I was found.…”

Section: 4 1 E T I a D Y T G K P T T I P G A V A I F E R Y A G P E mentioning

confidence: 99%

“…9, some similarity around the position of the 1,4-diamino-2-butyne-binding site of A. niger AO-I was found. But only bovine plasma amine oxidase [31] contains a lysyl residue in the same position as A. niger AO-I, although amine oxidases from Hansenula polymorpha [28] and Klebsiella aerogenes [30] also contain lysyl residues close to this position.…”

Section: 4 1 E T I a D Y T G K P T T I P G A V A I F E R Y A G P E mentioning

confidence: 99%

Active‐Site Covalent Modifications of Quinoprotein Amine Oxidases from Aspergillus niger

Frébort¹,

Peč

Luhová

et al. 1994

European Journal of Biochemistry

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Interactions of two distinct quinoprotein amine oxidases from Aspergillus niger, AO-I and AO-11, with active-site covalent modifiers have been investigated. Both enzymes are inhibited similarly by phenylhydrazine or p-nitrophenylhydrazine, forming an orange Schiff base with a carbonyl group of topaquinone cofactor. Modification of histidyl and tyrosyl residues by diethylpyrocarbonate and sulfhydryl groups by 5,5'-dithio-bis-(2-nitrobenzoic acid) and 4-chloro-7-nitrobenzo-2-oxa-l,3-diazole have been described. A substrate analog, 1,4-diamino-2-butyne, was found to function as a mechanism-based inhibitor. It shows both substrate saturation kinetics and time-dependent irreversible inhibition caused by formation of pynole bound to the active site. The pyrrole formation was confirmed spectrophotometrically by reaction with Ehrlich's reagent at 525 nm. Inhibition by 1,4-diamino-2-butyne produces a new maximum in the absorption spectra of AO-I and AO-I1 at 310 nm and 306 nm, respectively. Inactivated AO-I was digested by proteases ; labeled peptides were purified by C18 HPLC and sequenced by Edman degradation. Data reveal the evidence that 1P-diamino-2-butyne reacts with the &-amino group of the Lys356 residue in the sequence Lys-Met-Pro-AsnAla of Aspergillus niger amine oxidase AO-I.Amine oxidase of Aspergillus niger is a copper-carbonyl enzyme, which was found in the mid 1960s, purified and crystallized [l, 21. Copper and an undetermined carbonyl cofactor were found to function in the catalytic cycle [2-41. Nowadays, the importance of the fungal amine oxidase has risen again because the enzyme can be applied to monitor histamine contents in fishery products [5]. A massive production of the enzyme on the industrial scale has increased current interest.Recently, we have found two amine oxidases (EC 1.4.3.6), named AO-I and AO-11, in Aspergillus niger mycelia grown on n-butylamine medium [6, 71. AO-I is the enzyme previously reported, consisting of two 75-kDa subunits, while AO-I1 is a novel enzyme of 80 kDa. These amine oxidases do not show big differences in their peptide maps, but differ in their N-terminals. They also do not show any remarkable difference in substrate specificity or sensitivity to inhibitors. The cofactors of both enzymes give a typical reaction with p-nitrophenylhydrazine [6, 71 like other topaquiCorrespondence to I. Frkbort, Laboratory of Applied Microbiology, Faculty of Agriculture, Yarnaguchi University, 1 677-1 Yoshida, Yamaguchi, Japan 753Abbreviations. AO-I and AO-11, Aspergillus niger amine oxidases ; Nbs,, 5,5'-dithio-bis-(2-nitrobenzoic acid) ; buffer A, 0.01 M potassium phosphate pH 7.0.Enzymes. Amine oxidase, arnine:O, oxidoreductase (dearninating) (copper containing) (EC 1.4.3.6) ; peroxidase from horseradish (EC 1.11.1.7); pronase P from Streptomyces griseus (EC 3.4.24.31); thermolysin from Bacillus themolyticus rokko (EC 3.4.24.27 It is very probable that AO-I was purified and crystallized in earlier studies but fractions containing AO-I1 were not purified further because of its lower...

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“…In order to seek further evidence that the topogenic information of AMO indeed resides within its N-terminal 16 (AN 16AMO). To avoid misinterpretation of its subcellular sorting due to the synthesis of endogenous AMO, the truncated AMO protein was synthesized in an AMO disruption strain.…”

Section: A Short Deletion Of the N-termandus Of Amo Abolishes Peroxisommentioning

confidence: 99%

The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

et al. 1995

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Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

Cited by 87 publications

References 54 publications

Mutational Analysis of the Prt1 Protein Subunit of Yeast Translation Initiation Factor 3

Mutational Analysis of the Prt1 Protein Subunit of Yeast Translation Initiation Factor 3

Active‐Site Covalent Modifications of Quinoprotein Amine Oxidases from Aspergillus niger

The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

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