The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein

Hsieh, Yi-Ching; Tu, Pei-Jung; Lee, Ying-Yuan; Kuo, Chun-Chen; Lin, Yi-Chien; Wu, Chi-Fang; Lin, Jing‐Jer

doi:10.1042/bj20070968

Cited by 9 publications

(12 citation statements)

References 48 publications

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“…The ChIP analysis was conducted according to a described procedure (45). The Rap1p (SC-6662) antibody was purchased from Santa Cruz Biotechnology.…”

Section: Methodsmentioning

confidence: 99%

Telomeric transcripts stimulate telomere recombination to suppress senescence in cells lacking telomerase

Yu¹,

Kao

Lin

2014

Proc. Natl. Acad. Sci. U.S.A.

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109

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In human somatic cells or yeast cells lacking telomerase, telomeres are shortened upon each cell division. This gradual shortening of telomeres eventually leads to senescence. However, a small population of telomerase-deficient cells can survive by bypassing senescence through the activation of alternative recombination pathways to maintain their telomeres. Although genes involved in telomere recombination have been identified, mechanisms that trigger telomere recombination are less known. The THO (suppressor of the transcriptional defects of Hpr1 mutants by overexpression) complex is involved in transcription elongation and mRNA export. Here we demonstrate that mutations in THO complex components can stimulate early senescence and type II telomere recombination in cells lacking telomerase. The accumulation of telomere-associated noncoding telomere repeat-containing RNA (TERRA) is required for the observed telomere effects in THO complex mutants; reduced transcriptional efficiency, or overexpression of RNase H or C 1-3 A RNA can severely impair the type II telomere recombination. The results highlight a unique function for telomere-associated TERRA, in the formation of type II survivors. Moreover, because TERRA is a long noncoding RNA, these results reveal a function for long noncoding RNA in regulating recombination.

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“…The ChIP analysis was conducted according to a described procedure (45). The Rap1p (SC-6662) antibody was purchased from Santa Cruz Biotechnology.…”

Section: Methodsmentioning

confidence: 99%

Telomeric transcripts stimulate telomere recombination to suppress senescence in cells lacking telomerase

Yu¹,

Kao

Lin

2014

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

109

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“…The Imp4/Brix domain can associate with U3 small nucleolar RNA (snoRNA) and Mpp10, which are required for 35S pre-rRNA processing, to release 18S pre-rRNA and thus single-handedly initiate small subunit biogenesis ( 11 , 12 ). Moreover, single-stranded telomeric DNA has been reported to bind to the Imp4/Brix domain ( 13 ). A structural analysis of the Imp4-like protein Mil revealed the characteristic architecture of the Brix domain, which features a similar arrangement of structural elements in its N- and C-terminal halves ( 14 ).…”

Section: Introductionmentioning

confidence: 99%

Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis

Asano

Kato

Nakamura

et al. 2015

Nucleic Acids Research

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Proteins Rpf2 and Rrs1 are required for 60S ribosomal subunit maturation. These proteins are necessary for the recruitment of three ribosomal components (5S ribosomal RNA [rRNA], RpL5 and RpL11) to the 90S ribosome precursor and subsequent 27SB pre-rRNA processing. Here we present the crystal structure of the Aspergillus nidulans (An) Rpf2-Rrs1 core complex. The core complex contains the tightly interlocked N-terminal domains of Rpf2 and Rrs1. The Rpf2 N-terminal domain includes a Brix domain characterized by similar N- and C-terminal architecture. The long α-helix of Rrs1 joins the C-terminal half of the Brix domain as if it were part of a single molecule. The conserved proline-rich linker connecting the N- and C-terminal domains of Rrs1 wrap around the side of Rpf2 and anchor the C-terminal domain of Rrs1 to a specific site on Rpf2. In addition, gel shift analysis revealed that the Rpf2-Rrs1 complex binds directly to 5S rRNA. Further analysis of Rpf2-Rrs1 mutants demonstrated that Saccharomyces cerevisiae Rpf2 R236 (corresponds to R238 of AnRpf2) plays a significant role in this binding. Based on these studies and previous reports, we have proposed a model for ribosomal component recruitment to the 90S ribosome precursor.

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“…The Imp4 protein was shown to specifically bind single-stranded telomeric DNA and to associate with telomeres in vivo [17]. Whether the Imp3 and Mpp10 proteins are also required for tight binding of Imp4p to telomeres is yet unclear.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, an additional role of the U3 snoRNP was postulated in telomere function through the interaction between Imp4p and Cdc13p, a single-stranded telomere-binding protein involved in telomere maintenance [16] . The Imp4 protein was shown to specifically bind single-stranded telomeric DNA and to associate with telomeres in vivo [17] . Whether the Imp3 and Mpp10 proteins are also required for tight binding of Imp4p to telomeres is yet unclear.…”

Section: Introductionmentioning

confidence: 99%

A Viable Hypomorphic Allele of the Essential IMP3 Gene Reveals Novel Protein Functions in Saccharomyces cerevisiae

et al. 2011

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In Saccharomyces cerevisiae, the essential IMP3 gene encodes a component of the SSU processome, a large ribonucleoprotein complex required for processing of small ribosomal subunit RNA precursors. Mutation of the IMP3 termination codon to a sense codon resulted in a viable mutant allele producing a C-terminal elongated form of the Imp3 protein. A strain expressing the mutant allele displayed ribosome biogenesis defects equivalent to IMP3 depletion. This hypomorphic allele represented a unique opportunity to investigate and better understand the Imp3p functions. We demonstrated that the +1 frameshifting was increased in the mutant strain. Further characterizations revealed involvement of the Imp3 protein in DNA repair and telomere length control, pointing to a functional relationship between both pathways and ribosome biogenesis.

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The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein

Cited by 9 publications

References 48 publications

Telomeric transcripts stimulate telomere recombination to suppress senescence in cells lacking telomerase

Telomeric transcripts stimulate telomere recombination to suppress senescence in cells lacking telomerase

Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis

A Viable Hypomorphic Allele of the Essential IMP3 Gene Reveals Novel Protein Functions in Saccharomyces cerevisiae

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