2004
DOI: 10.1042/bj20040371
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Ribosomal protein L7a binds RNA through two distinct RNA-binding domains

Abstract: The human ribosomal protein L7a is a component of the major ribosomal subunit. We previously identified three nuclear-localization-competent domains within L7a, and demonstrated that the domain defined by aa (amino acids) 52-100 is necessary, although not sufficient, to target the L7a protein to the nucleoli. We now demonstrate that L7a interacts in vitro with a presumably G-rich RNA structure, which has yet to be defined. We also demonstrate that the L7a protein contains two RNA-binding domains: one encompass… Show more

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Cited by 31 publications
(31 citation statements)
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“…26 As shown in Figure 1C, the enforced expression of rpL3, in contrast to rpL7a, is associated to the upregulation of p21 gene promoter transactivation in a dose-dependent manner.…”
Section: Resultsmentioning
confidence: 99%
“…26 As shown in Figure 1C, the enforced expression of rpL3, in contrast to rpL7a, is associated to the upregulation of p21 gene promoter transactivation in a dose-dependent manner.…”
Section: Resultsmentioning
confidence: 99%
“…Brown II, personal communication] Currently, no detailed structural information is available for any eukaryotic L7a protein and its RNA-binding site (or motif) within the large subunit ribosomal RNA has not been defined. However, it does not appear that the human L7a protein can bind to a kink-turn motif (46). Differences in the amino acid sequence of L7a compared with Snu13p in the above-mentioned region (Figure 3B, overlined) are likely to contribute to the different RNA-binding properties displayed by the L7a protein.…”
Section: Resultsmentioning
confidence: 99%
“…Nuclear extracts was performed as previously reported4950, EMSA assay was performed as previously reported51.…”
Section: Methodsmentioning
confidence: 99%