<HashMap><database>biostudies-other</database><scores/><additional><submitter>Bergemann AD</submitter><funding>NCI NIH HHS</funding><pagination>5673-82</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC360507</full_dataset_link><abstract>The human Pur factor binds strongly to a sequence element repeated within zones of initiation of DNA replication in several eukaryotic cells. The protein binds preferentially to the purine-rich single strand of this element, PUR. We report here the cloning and sequencing of a cDNA encoding a protein with strong affinity for the PUR element. Analysis with a series of mutated oligonucleotides defines a minimal single-stranded DNA Pur-binding element. The expressed Pur open reading frame encodes a protein of 322 amino acids. This protein, Pur alpha, contains three repeats of a consensus motif of 23 amino acids and two repeats of a second consensus motif of 26 amino acids. Near its carboxy terminus, the protein possesses an amphipathic alpha-helix and a glutamine-rich domain. The repeat region of Pur cDNA is homologous to multiple mRNA species in each of several human cell lines and tissues. The HeLa cDNA library also includes a clone encoding a related gene, Pur beta, containing a version of the 23-amino-acid consensus motif similar, but not identical, to those in Pur alpha. Results indicate a novel type of modular protein with capacity to bind repeated elements in single-stranded DNA.</abstract><repository>biostudies-other</repository><data_source>Europe PMC</data_source><omics_type>Unknown</omics_type><volume>12(12)</volume><journal>Molecular and cellular biology</journal><pmcid>PMC360507</pmcid><funding_grant_id>CA55219</funding_grant_id><pubmed_authors>Ma ZW</pubmed_authors><pubmed_authors>Bergemann AD</pubmed_authors><pubmed_authors>Johnson EM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Sequence of cDNA comprising the human pur gene and sequence-specific single-stranded-DNA-binding properties of the encoded protein.</name><description>The human Pur factor binds strongly to a sequence element repeated within zones of initiation of DNA replication in several eukaryotic cells. The protein binds preferentially to the purine-rich single strand of this element, PUR. We report here the cloning and sequencing of a cDNA encoding a protein with strong affinity for the PUR element. Analysis with a series of mutated oligonucleotides defines a minimal single-stranded DNA Pur-binding element. The expressed Pur open reading frame encodes a protein of 322 amino acids. This protein, Pur alpha, contains three repeats of a consensus motif of 23 amino acids and two repeats of a second consensus motif of 26 amino acids. Near its carboxy terminus, the protein possesses an amphipathic alpha-helix and a glutamine-rich domain. The repeat region of Pur cDNA is homologous to multiple mRNA species in each of several human cell lines and tissues. The HeLa cDNA library also includes a clone encoding a related gene, Pur beta, containing a version of the 23-amino-acid consensus motif similar, but not identical, to those in Pur alpha. Results indicate a novel type of modular protein with capacity to bind repeated elements in single-stranded DNA.</description><dates><release>1992-01-01T00:00:00Z</release><publication>1992 Dec</publication><modification>2019-03-27T00:50:09Z</modification><creation>2019-03-27T00:50:09Z</creation></dates><accession>S-EPMC360507</accession><cross_references><gen>M96684</gen><pubmed>1448097</pubmed><doi>10.1128/MCB.12.12.5673 </doi></cross_references></HashMap>