DNA-nuclease activity of the single-chain ribosome-inactivating proteins dianthin 30, saporin 6 and gelonin

L. Roncuzzi; A. Gasperi-Campani

doi:10.1016/0014-5793(96)00776-4

DNA-nuclease activity of the single-chain ribosome-inactivating proteins dianthin 30, saporin 6 and gelonin

L. Roncuzzi, A. Gasperi-Campani

Istituti Ortopedici Rizzoli

Research output: Contribution to journal › Article › peer-review

Abstract

The single-chain ribosome-inactivating proteins (sc-RIPs) from plant origin are antiviral and antiproliferative agents employed in the preparation of immunotoxins, Similarly to the A-chains of ricin, sc-RIPs act as rRNA N-glycosidases. We demonstrate here that dianthin 30, saporin 6 and gelonin exert a specific nuclease activity on supercoiled DNA. Four specific sites of cleavage introduced by dianthin 30 and by saporin 6 and two specific sites of cleavage introduced by gelonin have been identified and mapped in pBR322.

Original language	English
Pages (from-to)	16-20
Number of pages	5
Journal	FEBS Letters
Volume	392
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(96)00776-4
Publication status	Published - Aug 19 1996

Keywords

Dianthin 30
DNAse activity
Gelonin
Ribosome-inactivating protein
Saporin 6
Supercoiled DNA

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0014-5793(96)00776-4

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abstract = "The single-chain ribosome-inactivating proteins (sc-RIPs) from plant origin are antiviral and antiproliferative agents employed in the preparation of immunotoxins, Similarly to the A-chains of ricin, sc-RIPs act as rRNA N-glycosidases. We demonstrate here that dianthin 30, saporin 6 and gelonin exert a specific nuclease activity on supercoiled DNA. Four specific sites of cleavage introduced by dianthin 30 and by saporin 6 and two specific sites of cleavage introduced by gelonin have been identified and mapped in pBR322.",

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AU - Roncuzzi, L.

AU - Gasperi-Campani, A.

PY - 1996/8/19

Y1 - 1996/8/19

N2 - The single-chain ribosome-inactivating proteins (sc-RIPs) from plant origin are antiviral and antiproliferative agents employed in the preparation of immunotoxins, Similarly to the A-chains of ricin, sc-RIPs act as rRNA N-glycosidases. We demonstrate here that dianthin 30, saporin 6 and gelonin exert a specific nuclease activity on supercoiled DNA. Four specific sites of cleavage introduced by dianthin 30 and by saporin 6 and two specific sites of cleavage introduced by gelonin have been identified and mapped in pBR322.

AB - The single-chain ribosome-inactivating proteins (sc-RIPs) from plant origin are antiviral and antiproliferative agents employed in the preparation of immunotoxins, Similarly to the A-chains of ricin, sc-RIPs act as rRNA N-glycosidases. We demonstrate here that dianthin 30, saporin 6 and gelonin exert a specific nuclease activity on supercoiled DNA. Four specific sites of cleavage introduced by dianthin 30 and by saporin 6 and two specific sites of cleavage introduced by gelonin have been identified and mapped in pBR322.

KW - Dianthin 30

KW - DNAse activity

KW - Gelonin

KW - Ribosome-inactivating protein

KW - Saporin 6

KW - Supercoiled DNA

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DNA-nuclease activity of the single-chain ribosome-inactivating proteins dianthin 30, saporin 6 and gelonin

Abstract

Keywords

ASJC Scopus subject areas

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