Subscribe to RSS
DOI: 10.1055/s-2008-1034371
© Georg Thieme Verlag KG Stuttgart · New York
N-Terminal Amino Acid Sequences of Intact and Cleaved Forms of Mung Bean Nuclease
Publication History
Received: November 26, 2007
Revised: January 10, 2008
Accepted: February 24, 2008
Publication Date:
01 April 2008 (online)
Abstract
We report, for the first time, the N-terminal amino acid sequences of both intact and cleaved forms (fragments A and B) of Mung bean nuclease, purified from sprouts of Vigna radiata or purchased from Amersham Biosciences. The N-terminal sequence of Mung bean nuclease shows high similarity with the putative bifunctional nuclease from Arabidopsis thaliana (AC: AAM63596).
Abbreviations
MBN:Mung bean nuclease
PAGE:polyacrylamide gel electrophoresis
PVDF:poly(vinylidene difluoride)
SDS:sodium dodecyl sulfate
Key words
Mung bean nuclease - Vigna radiata - Fabaceae - ribosome-inactivating protein - Edman degradation
References
- 1 Chin J, Banaszczyk M, Jubian V, Zou X. Co(III) complex promoted hydrolysis of phosphate diesters: comparison in reactivity of rigid cis-diaquotetraazacobalt(III) complexes. J Am Chem Soc. 1989; 111 186-90
- 2 Serpersu E H, Shortle D, Mildvan A S. Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis. Biochemistry. 1987; 26 1289-300
- 3 Gerlt J A. Mechanistic principles of enzyme-catalyzed cleavage of phosphodiester bonds. In: Linn SM, Lloyd RS, Roberts RJ, editors. Nucleases, 2nd edition. Cold Spring Harbor: Cold Spring Harbor Laboratory. Press; 1993 1-34
- 4 Laskowski M S r. Purification and properties of the Mung bean nuclease. Methods Enzymol. 1980; 65 263-76
- 5 Sung S C, Laskowski M S r. A Mung bean nuclease from sprouts. J Biol Chem. 1962; 237 506-11
- 6 Kowalski D, Kroeker W D, Laskowski M S r. Mung bean nuclease I. Physical, chemical, and catalytic properties. Biochemistry. 1976; 15 4457-63
- 7 Desai N A, Shankar V. Single-strand-specific nucleases. FEMS Microbiol Rev. 2003; 26 457-91
- 8 Aceto A, Di Maro A, Conforto B, Siniscalco S G, Parente A, Delli Bovi P. et al . Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves. Biol Chem. 2005; 386 307-17
- 9 Yaw-Huei L, Wen-Hsiang Y. Mung bean (Vigna radiata L. Wilczek) contains some high proteolytic activities already before germination. Bot Bull Acad Sin. 1996; 37 1-7
- 10 Di Maro A, Del Vecchio Blanco F, Savino G, Parente A. Isolation and characterization of a nicked form of the single-chain ribosome inactivating protein from seeds of Phytolacca dioica L. First European Symposium of the Protein Society Davos; 1995
- 11 Sheldon P S, Keen J N, Bowles D J. Post-translational peptide bond formation during concanavalin A processing in vitro. . Biochem J. 1996; 15 865-70
- 12 Laemmli U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227 680-5
- 13 Di Maro A, Ferranti P, Mastronicola M, Polito L, Bolognesi A, Stirpe F. et al . Reliable sequence determination of ribosome-inactivating proteins by combining electrospray mass spectrometry and Edman degradation. J Mass Spectrom. 2001; 36 38-46
Antimo Di Maro
Dipartimento di Scienze della Vita
Seconda Università degli Studi di Napoli
I-81100 Caserta
Italy
Phone: +39-0823-274-535
Fax: +39-0823-274-571
Email: antimo.dimaro@unina2.it