ArticleMolecular and cellular biology1999
Gbp1p, a protein with RNA recognition motifs, binds single-stranded telomeric DNA and changes its binding specificity upon dimerization.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Molecular characterization ofLife science alliance · 2019Article
- Expression profile of telomere-associated genes in multiple myeloma.Journal of cellular and molecular medicine · 2012Article
- Activation of the carbon concentrating mechanism by CO2 deprivation coincides with massive transcriptional restructuring in Chlamydomonas reinhardtii.The Plant cell · 2012Article
- The role of an E-box element: multiple frunctions and interacting partners.Plant signaling & behavior · 2010Review
- Multiple roles and interaction factors of an E-box element in Chlamydomonas reinhardtii.Plant physiology · 2010Article
- Hierarchical mechanisms build the DNA-binding specificity of FUSE binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Subcellular distribution of human RDM1 protein isoforms and their nucleolar accumulation in response to heat shock and proteotoxic stress.Nucleic acids research · 2007Article
- Novel DNA-binding properties of the RNA-binding protein TIAR.Nucleic acids research · 2005Article
- A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation.Oncogene · 2002Review
- Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with the RNA component of human telomerase.Molecular and cellular biology · 2000Article
- The Est1 subunit of yeast telomerase binds the Tlc1 telomerase RNA.Molecular and cellular biology · 2000Article
- Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA.Genes & development · 1999Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Gbp1p is a putative telomere-binding protein from Chlamydomonas reinhardtii that contains two RNA recognition motifs (RRMs) which are commonly found in heterogeneous nuclear ribonucleoproteins (hnRNPs). Previously we demonstrated that Gbp1p binds single-stranded DNA (ssDNA) containing the Chlamydomonas telomeric sequence but not the RNA containing the cognate sequence. Here we show that at lower protein concentrations Gbp1 can also bind an RNA containing the cognate sequence. We found that mutation of the two RRM motifs of Gbp1p to match the highly conserved region of hnRNP RRMs did not alter the affinity of Gbp1p for either RNA or DNA. The ability of Gbp1p to associate with either of these two nucleic acids is governed by the dimerization state of the protein. Monomeric Gbp1p associates with either ssDNA or RNA, showing a small binding preference for RNA. Dimeric Gbp1p has a strong preference for binding ssDNA and shows little affinity for RNA. To the best of our knowledge, this is the first example of a protein that qualitatively shifts its nucleic acid binding preference upon dimerization. The biological implications of a telomere-binding protein that is regulated by dimerization are discussed.
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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.