ArticleThe Journal of cell biology1995
A zinc-binding domain is required for targeting the maternal nuclear protein PwA33 to lampbrush chromosome loops.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- DENR-MCTS1 heterodimerization and tRNA recruitment are required for translation reinitiation.PLoS biology · 2018Article
- The vertebrate makorin ubiquitin ligase gene family has been shaped by large-scale duplication and retroposition from an ancestral gonad-specific, maternal-effect gene.BMC genomics · 2010Article
- The tripartite motif of nuclear factor 7 is required for its association with transcriptional units.Molecular and cellular biology · 2007Article
- PML protein isoforms and the RBCC/TRIM motif.Oncogene · 2001Review
- The tripartite motif family identifies cell compartments.The EMBO journal · 2001Article
- Article
- Coilin can form a complex with the U7 small nuclear ribonucleoprotein.Molecular biology of the cell · 1998Article
- Assembly of lampbrush chromosomes from sperm chromatin.Molecular biology of the cell · 1998Article
- Structural organization and mammary-specific expression of the butyrophilin gene.Mammalian genome : official journal of the International Mammalian Genome Society · 1996Article
- In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In oocytes of the newt Pleurodeles waltl, the maternal nuclear protein PwA33 occurs on the lampbrush chromosomes and in some nucleoplasmic particles of the germinal vesicle. PwA33 is a modular protein and we used site-directed mutagenesis to alter the sequences encoding two metal-binding regions, the C3HC4 (or RING finger) and B-box motifs. Several mutant clones were generated and their synthetic transcripts were injected into Pleurodeles oocytes for in vivo analysis. In the oocyte, all translation products localized in the germinal vesicle. Proteins encoded by RING finger mutant clones were distributed in a pattern identical to that of the wild type protein, but when His266 of the B-box was mutated, PwA33 failed to localize in the lampbrush chromosomes and the nucleoplasmic particles. Using an in vitro colorimetric assay, we demonstrated that PwA33 is a zinc-binding protein and that mutations in the RING finger and B-Box altered its metal-binding properties. The RING finger motif bound two Zn2+ ions and the binding ratios of several mutants were consistent with the tertiary structure recently proposed for this motif. The B-box coordinated one Zn2+ and this binding was inhibited by the His266 mutation. The failure of the His266 mutation to bind zinc and to localize properly within the germinal vesicle suggests that an intact B-box is required for normal functioning of the PwA33 protein in the oocyte.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.