Metal selectivity studies of the cation diffusion facilitator protein family

S. Barber-Zucker; B. Shaanan; R. Zarivach

doi:10.1111/febs.14174

Metal selectivity studies of the cation diffusion facilitator protein family

S. Barber-Zucker, B. Shaanan, R. Zarivach

Department of Life Sciences

Ben-Gurion University of the Negev

Research output: Contribution to journal › Meeting Abstract

Abstract

The restriction endonuclease CglI from Corynebacterium glutamicum recognizes an asymmetric 50–GCCGC–30 site and cleaves the DNA 7 and 6/7 nucleotides downstream on the top and bottom DNA strands, respectively, in an NTP–hydrolysis depen-dent reaction. CglI is composed of two different proteins: anendonuclease (R.CglI) and a DEAD–family helicase–like ATPase(H.CglI).

Original language	American English
Article number	P.3.1.A-004
Pages (from-to)	205-205
Number of pages	1
Journal	FEBS Journal
Volume	284
DOIs	https://doi.org/10.1111/febs.14174
State	Published - Sep 2017

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10.1111/febs.14174

Cite this

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title = "Metal selectivity studies of the cation diffusion facilitator protein family",

abstract = "The restriction endonuclease CglI from Corynebacterium glutamicum recognizes an asymmetric 50–GCCGC–30 site and cleaves the DNA 7 and 6/7 nucleotides downstream on the top and bottom DNA strands, respectively, in an NTP–hydrolysis depen-dent reaction. CglI is composed of two different proteins: anendonuclease (R.CglI) and a DEAD–family helicase–like ATPase(H.CglI).",

author = "S. Barber-Zucker and B. Shaanan and R. Zarivach",

year = "2017",

month = sep,

doi = "10.1111/febs.14174",

language = "American English",

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journal = "FEBS Journal",

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T1 - Metal selectivity studies of the cation diffusion facilitator protein family

AU - Barber-Zucker, S.

AU - Shaanan, B.

AU - Zarivach, R.

PY - 2017/9

Y1 - 2017/9

N2 - The restriction endonuclease CglI from Corynebacterium glutamicum recognizes an asymmetric 50–GCCGC–30 site and cleaves the DNA 7 and 6/7 nucleotides downstream on the top and bottom DNA strands, respectively, in an NTP–hydrolysis depen-dent reaction. CglI is composed of two different proteins: anendonuclease (R.CglI) and a DEAD–family helicase–like ATPase(H.CglI).

AB - The restriction endonuclease CglI from Corynebacterium glutamicum recognizes an asymmetric 50–GCCGC–30 site and cleaves the DNA 7 and 6/7 nucleotides downstream on the top and bottom DNA strands, respectively, in an NTP–hydrolysis depen-dent reaction. CglI is composed of two different proteins: anendonuclease (R.CglI) and a DEAD–family helicase–like ATPase(H.CglI).

U2 - 10.1111/febs.14174

DO - 10.1111/febs.14174

M3 - Meeting Abstract

SN - 1742-464X

VL - 284

SP - 205

EP - 205

JO - FEBS Journal

JF - FEBS Journal

M1 - P.3.1.A-004

ER -