Premium
Common structural features of replication origins in all life forms
Author(s) -
Boulikas Teni
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19960301)60:3<297::aid-jcb2>3.0.co;2-r
Subject(s) - biology , dna replication , dna , origin recognition complex , control of chromosome duplication , primase , microbiology and biotechnology , eukaryotic dna replication , genetics , rna , reverse transcriptase , gene
Origins of replication (ORIs) among prokaryotes, viruses, and multicellular organisms appear to possess simple tri‐, tetra‐, or higher dispersed repetitions of nucleotides, AT tracts, inverted repeats, one to four binding sites of an initiator protein, intrinsically curved DNA, DNase I‐hypersensitive sites, a distinct pattern of DNA methylation, and binding sites for transcription factors. Eukaryotic ORIs are sequestered on the nuclear matrix; this attachment is supposed to facilitate execution of their activation/deactivation programs during development. Furthermore, ORIs fall into various classes with respect to their sequence complexity: those enriched in AT tracts, those with GA‐ and CT‐rich tracts, a smaller class of GC‐rich ORIs, and a major class composed of mixed motifs yet containing distinct AT and polypurine or GC stretches. Multimers of an initiator protein in prokaryotes and viruses that might have evolved into a multiprotein replication initiation complex in multicellular organisms bind to the core ORI, causing a structural distortion to the DNA which is transferred to the AT tract flanking the initiator protein site; single‐stranded DNA‐binding proteins then interact with the melted AT tract as well as with the DNA polymerase α‐primase complex in animal viruses and mammalian cells, causing initiation in DNA replication. ORIs in mammalian cells seem to colocalize with matrix‐attached regions and are proposed to become DNase I‐hypersensitive during their activation. © 1996 Wiley‐Liss, Inc.