NDLI: Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family.

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Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family.

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Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gorbalenya, A. E.
Description	Author Affiliation: Gorbalenya AE ( Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region.)
Abstract	A new family of protein domains consisting of 50-80 amino acid residues is described. It is composed of nearly 40 members, including domains encoded by plastid and phage group I introns; mitochondrial, plastid, and bacterial group II introns; eubacterial genomes and plasmids; and phages. The name 'EX1HH-HX3H' was coined for both domain and family. It is based on 2 most prominent amino acid sequence motifs, each encompassing a pair of highly conserved histidine residues in a specific arrangement: EX1HH and HX3H. The 'His' motifs often alternate with amino- and carboxy-terminal motifs of a new type of Zn-finger-like structure CX2,4CX29-54[CH]X2,3[CH]. The EX1HH-HX3H domain in eubacterial E2-type bacteriocins and in phage RB3 (wild variant of phage T4) product of the nrdB group I intron was reported to be essential for DNA endonuclease activity of these proteins. In other proteins, the EX1HH-HX3H domain is hypothesized to possess DNase activity as well. Presumably, this activity promotes movement (rearrangement) of group I and group II introns encoding the EX1HH-HX3H domain and other gene targets. In the case of Escherichia coli restrictase McrA and possibly several related proteins, it appears to mediate the restriction of alien DNA molecules.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	7
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Deoxyribonucleases Genetics Introns Rna Splicing Amino Acid Sequence Conserved Sequence Chemistry Histidine Molecular Sequence Data Sequence Alignment Zinc Metabolism Zinc Fingers Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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