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Findings indicate the function of tumor suppressor protein p53 (p53 (show TP53 Proteins)) and DNA polymerase iota (POLiota) in the DNA damage response to endogenous or exogenous replication stress.
DNA polymerase iota increased the expression of MMP-2 (show MMP2 Proteins)/9 to promote invasion and metastasis of esophageal squamous cell carcinoma.
Data suggest that error-free DNA replication through 3-deaza-3-methyladenine adduct is mediated via three different pathways dependent upon POL-iota/POL-kappa, POL-theta, and POL-zeta.
Kinetic and Structural Impact of Metal Ions and Genetic Variations on Human DNA Polymerase iota.
Germline genetic variations in human POLI gene may either hinder or promote the translesion synthesis (TLS (show FUS Proteins)) capability of pol iota (show POLM Proteins) with various DNA lesions in vitro, emphasizing the potential translational importance of these pol iota (show POLM Proteins) genetic variations, e.g., individual differences in TLS (show FUS Proteins), mutation, and cancer susceptibility to genotoxic carcinogens.
a single residue in pol iota (show POLM Proteins) is able to discriminate between NTPs and dNTPs during DNA synthesis.
Dysregulation of pol iota (show POLM Proteins) by JNK/c-Jun is involved in carcinogenesis and offer a novel understanding of the role of pol iota (show POLM Proteins) or c-Jun (show JUN Proteins) in mutagenesis.
Human Pol iota and yeast Pol zeta complex could function efficiently in the insertion and extension steps, respectively, of ranslesion synthesis and human Pol kappa and Pol eta could also extend past these lesions, albeit much less efficiently.
POLI and MC4R (show MC4R Proteins) nearby single nucleotide polymorphisms in human chromosome 18 are associated with a moderate risk of type 2 diabetes.
Results show that the physical and functional interaction between pols eta and iota occurs between ubiquitinated forms of either polymerase via their respective ubiquitin-binding domains.
Pol iota occasionally accesses the replication fork to generate a first mutation, and Pol zeta extends the mismatch with a second mutation.
Mouse DNA polymerase iota lacking exon 2 (42 amino acids) is catalytically inactive in vitro.
Exon 2 deletion abrogates both the DNA polymerase (show POLB Proteins) and dRP lyase activities of Pol iota in the presence of either Mg(2 (show MCOLN1 Proteins)+) or Mn(2+) ions. Thus, 129-derived strains of mice express catalytically inactive alternatively spliced Pol iota variant.
PolH (show POLH Proteins) contributes to accurate translesion synthesis (TLS (show FUS Proteins)) past both T- & C-containing dimers. PolI is involved in error-prone TLS (show FUS Proteins) past cytosine-containing dimers when Poleta is inactivated.
Poliota causes the Par2 (show F2RL1 Proteins) effect and inhibits tumorigenesis and mutagenesis
Upon DNA damage, the UBDs (UBM domains) of polymerase iota (Pol iota) interact with ubiquitinated proliferating cell nuclear antigen (show PCNA Proteins) to regulate the interchange between processive DNA polymerases and translesional synthesis
In the presence of Mg2 (show MCOLN1 Proteins)+, the enzyme was active only in testicles and brain, whereas in the presence of Mn2+ the activity was found in all organs.
Data suggest that either DNA polymerase iota does not participate in hypermutation, or its role is nonessential and can be readily assumed by another low-fidelity polymerase.
Nucleotide polymorphisms in DNA polymerase iota is associated with lung tumorigenesis in mouse and humans
Pol kappa (show POLL Proteins) and Pol iota double-deficient mice had the normal somatic hypermutation frequency
Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity).
DNA polymerase iota
, polymerase (DNA directed) iota
, DNA polymerase iota-like
, RAD30 homolog B
, polymerase (DNA-directed), iota