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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-10-11
pubmed:abstractText
The roles of certain amino acids within zinc finger peptides of the Cys2His2 type in determining DNA-binding site specificity were investigated. A variety of three domain peptides designed using a consensus sequence framework were prepared with different potential DNA-contacting residues and tested in a recently developed specificity determination assay. Proteins with recognition helix sequence Q-1S1S2N3L4Q5K6 and QSSDLQK prefer binding subsites 5'-GAA-3' and 5'-(G/T)C(A/G)-3', respectively. Changing the Ser residues in position 2 to Ala in these proteins did not significantly affect the DNA binding site preferences, indicating that Ser residues, which occur frequently in position 2 in known zinc finger proteins are not, in general, responsible for determining binding site preferences. Examination of proteins with recognition helices HSSNLQK and ASSNLQK revealed considerable loss of binding site discrimination throughout the binding subsite. These observations provide further evidence for the importance of residues in positions -1 and 3 in determining DNA binding specificity. Moreover, these results illustrate the effects of changes of one residue in the recognition helix on binding site preferences throughout the recognition subsite.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-5
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Serine at position 2 in the DNA recognition helix of a Cys2-His2 zinc finger peptide is not, in general, responsible for base recognition.
pubmed:affiliation
Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.
pubmed:publicationType
Journal Article