The modification of tyrosyl residues of a minor ribonuclease from Aspergillus saitoi.

Watanabe, Hideaki; Sugiyama, Sakae; Nakamoto, Yoshimi; Matsuno, Kyoko; Ohgi, Kazuko; Irie, Masachika

doi:10.1248/cpb.33.4500

Cited by 3 publications

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“…2. The highest degrees of similarity were found with the periplasmic RNase I of E. coli (31) and the excreted RNases M ofAspergillus saitoi (57), T2 of Aspergillus oryzae (22), and Rh of Rhizopus niveus (13). By using the shared motif HGLWP, a search of the SWISSPROT 20 data base allowed the further identification of RNase LE of Lycopersicon esculentum (20) induction time of DH5a (pSSVI48-22) from 60 to 120 or 240 min resulted in an enrichment of cytoplasmic activity relative to that in the periplasm (data not shown).…”

Section: Methodsmentioning

confidence: 99%

Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases

1993

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The isolation, sequencing, and characterization of a periplasmic RNase gene from Aeromonas hydrophila AH1133 is described. Following subcloning of the gene on a 2.7-kb PstI fragment, its direction of transcription and approximate location were determined. Analysis of the nucleotide sequence reveals that the gene is 645 bp long, coding for 215 amino acid residues with a total molecular weight of 24,215. A typical leader sequence is present at the beginning of the corresponding protein. Computer analysis revealed strong local similarities to Escherichia coli RNase I and to the active site of a family of eukaryotic RNases. Expression studies indicate that the RNase natural promoter functions poorly in E. coli. In this organism, the enzyme is mainly localized in the cytoplasm and periplasm, although high levels of expression lead to significant release into the extracellular medium. Functional and physical characterizations further indicate that the periplasmic and cytoplasmic enzymes of A. hydrophila are likely to be the counterparts of E. coli RNase I and its cytoplasmic form RNase I*: as for the E. coli enzymes, the A. hydrophila RNase forms have similar sizes and show broad specificity, and the periplasmic form is more active towards natural polymer RNA than its cytoplasmic counterpart. Both forms are relatively thermosensitive and are reversibly inactivated by up to 0.6% sodium dodecyl sulfate. Southern hybridization revealed homology to E. coli K-12 and Shigella sp. genomic DNA, a finding which correlates with the presence of secreted RNases in these organisms. In contrast, species of phylogenetically closer genera, such as Vibrio and Pksiomonas, did not hybridize to the A. hydrophila RNase gene.

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Section: Methodsmentioning

confidence: 99%

Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases

1993

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“…5) These residues are completely conserved in RNase Po1 except for Tyr45 (RNase T1) being changed to Phe (RNase Po1). A comparison of the primary structures of RNase Po1 and RNase T1 and other RNase T1 family RNases shows that RNase T1 contains four cysteine residues that form two disulfide bonds, whereas RNase Po1 has six cysteine residues 1,[8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23] (Fig. 1).…”

mentioning

confidence: 99%

X-Ray Crystallographic Structure of RNase Po1 That Exhibits Anti-tumor Activity

Kobayashi

Katsutani

Hara

et al. 2014

Biological & Pharmaceutical Bulletin

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RNase Po1 is a guanylic acid-specific ribonuclease member of the RNase T1 family from Pleurotus ostreatus. We previously reported that RNase Po1 inhibits the proliferation of human tumor cells, yet RNase T1 and other T1 family RNases are non-toxic. We determined the three-dimensional X-ray structure of RNase Po1 and compared it with that of RNase T1. The catalytic sites are conserved. However, there are three disulfide bonds, one more than in RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. A comparison of the electrostatic potential of the molecular surfaces of these two proteins shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically. We suggest that the structural stability and cationic character of RNase Po1 are critical to the anti-cancer properties of the protein.

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The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T₁

Flögel¹,

Zielenkiewicz²

1988

FEBS Letters

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Ribonuclease MS from Aspergillus saitoi is a small acidic protein (117 14 Da) containing 106 amino acids of known sequence. Unlike other enzymes belonging to the RNase T, family this rihonuclease is base-unspecific. Using interactive computer graphics and energy minimisation we predicted the structure of RNase MS on the basis of sequence homology to RNase T1 of known structure. In this report the predicted structure of this protein is presented and character&d.

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The modification of tyrosyl residues of a minor ribonuclease from Aspergillus saitoi.

Cited by 3 publications

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Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases

Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases

X-Ray Crystallographic Structure of RNase Po1 That Exhibits Anti-tumor Activity

The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T₁

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The modification of tyrosyl residues of a minor ribonuclease from Aspergillus saitoi.

Cited by 3 publications

References 0 publications

Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases

Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases

X-Ray Crystallographic Structure of RNase Po1 That Exhibits Anti-tumor Activity

The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T1

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The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T₁