Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin

Emmanuelle Nicolas; Joseph M. Beggs; Brett M. Haltiwanger; Theodore F. Taraschi

doi:10.1016/S0014-5793(97)00267-6

Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin

Emmanuelle Nicolas
, Joseph M. Beggs
, Brett M. Haltiwanger
, Theodore F. Taraschi

Cancer Signaling and Microenvironment (CSM)

Jefferson Medical College

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

43 Scopus citations

Abstract

Several plant ribotoxins, including gelonin, were reported to have additional weak nuclease activities on supercoiled DNA. The potential contribution of this activity to their cytotoxicity has not been given serious consideration due to concerns about contaminating nucleases in the protein preparations. We now report the degradation of single-stranded DNA by preparations of native plant gelonin and recombinant gelonin produced in E. coli. The DNase activity of both preparations is similarly modulated by zinc. An SDS-PAGE DNase assay identifies gelonin as the polypeptide responsible for deoxyribonuclease activity.

Original language	English
Pages (from-to)	162-164
Number of pages	3
Journal	FEBS Letters
Volume	406
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(97)00267-6
State	Published - Apr 7 1997

Keywords

DNA, Single-Stranded/drug effects
Deoxyribonucleases/metabolism
Plant Proteins/metabolism
Plants/metabolism
Recombinant Proteins/metabolism
Ribosome Inactivating Proteins, Type 1
Ribosomes/drug effects

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10.1016/S0014-5793(97)00267-6

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title = "Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin",

abstract = "Several plant ribotoxins, including gelonin, were reported to have additional weak nuclease activities on supercoiled DNA. The potential contribution of this activity to their cytotoxicity has not been given serious consideration due to concerns about contaminating nucleases in the protein preparations. We now report the degradation of single-stranded DNA by preparations of native plant gelonin and recombinant gelonin produced in E. coli. The DNase activity of both preparations is similarly modulated by zinc. An SDS-PAGE DNase assay identifies gelonin as the polypeptide responsible for deoxyribonuclease activity.",

keywords = "DNA, Single-Stranded/drug effects, Deoxyribonucleases/metabolism, Plant Proteins/metabolism, Plants/metabolism, Recombinant Proteins/metabolism, Ribosome Inactivating Proteins, Type 1, Ribosomes/drug effects",

author = "Emmanuelle Nicolas and Beggs, \{Joseph M.\} and Haltiwanger, \{Brett M.\} and Taraschi, \{Theodore F.\}",

year = "1997",

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doi = "10.1016/S0014-5793(97)00267-6",

language = "English",

volume = "406",

pages = "162--164",

journal = "FEBS Letters",

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T1 - Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin

AU - Nicolas, Emmanuelle

AU - Beggs, Joseph M.

AU - Haltiwanger, Brett M.

AU - Taraschi, Theodore F.

PY - 1997/4/7

Y1 - 1997/4/7

N2 - Several plant ribotoxins, including gelonin, were reported to have additional weak nuclease activities on supercoiled DNA. The potential contribution of this activity to their cytotoxicity has not been given serious consideration due to concerns about contaminating nucleases in the protein preparations. We now report the degradation of single-stranded DNA by preparations of native plant gelonin and recombinant gelonin produced in E. coli. The DNase activity of both preparations is similarly modulated by zinc. An SDS-PAGE DNase assay identifies gelonin as the polypeptide responsible for deoxyribonuclease activity.

AB - Several plant ribotoxins, including gelonin, were reported to have additional weak nuclease activities on supercoiled DNA. The potential contribution of this activity to their cytotoxicity has not been given serious consideration due to concerns about contaminating nucleases in the protein preparations. We now report the degradation of single-stranded DNA by preparations of native plant gelonin and recombinant gelonin produced in E. coli. The DNase activity of both preparations is similarly modulated by zinc. An SDS-PAGE DNase assay identifies gelonin as the polypeptide responsible for deoxyribonuclease activity.

KW - DNA, Single-Stranded/drug effects

KW - Deoxyribonucleases/metabolism

KW - Plant Proteins/metabolism

KW - Plants/metabolism

KW - Recombinant Proteins/metabolism

KW - Ribosome Inactivating Proteins, Type 1

KW - Ribosomes/drug effects

UR - https://www.scopus.com/pages/publications/0030992505

U2 - 10.1016/S0014-5793(97)00267-6

DO - 10.1016/S0014-5793(97)00267-6

M3 - Article

C2 - 9109409

AN - SCOPUS:0030992505

SN - 0014-5793

VL - 406

SP - 162

EP - 164

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin

Abstract

Keywords

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