The iron chaperone and nucleic acid-binding activities of poly(rC)-binding protein 1 are separable and independently essential.

ABSTRACT: Poly(rC)-binding protein (PCBP1) is a multifunctional adaptor protein that can coordinate single-stranded nucleic acids and iron-glutathione complexes, altering the processing and transfer of these ligands through interactions with other proteins. Multiple phenotypes are ascribed to cells lacking PCBP1, but the relative contribution of RNA, DNA, or iron chaperone activity is not consistently clear. Here, we report the identification of amino acid residues required for iron coordination on each structural domain of PCBP1 and confirm the requirement of iron coordination for binding target proteins BolA2 and ferritin. We further construct PCBP1 variants that lack either nucleic acid- or iron-binding activity and examine their functions in human cells and mouse tissues depleted of endogenous P

SUBMITTER: Patel SJ 

PROVIDER: S-EPMC8237648 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature