The nuclear gene <i>HCF107</i> encodes a membrane‐associated R‐TPR (RNA tetratricopeptide repeat)‐containing protein involved in expression of the plastidial <i>psbH</i> gene in Arabidopsis

Sane, Aniruddha P.; Stein, Bernhard; Westhoff, Peter

doi:10.1111/j.1365-313x.2005.02409.x

Cited by 65 publications

(59 citation statements)

References 52 publications

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“…Crystal structures of CstF-77 confirmed that HAT repeat tracts adopt a TPR-like structure (3,4). The possibility that HAT repeat tracts might bind RNA has been suggested (1,(5)(6)(7), but the notion that HAT repeat tracts serve as a scaffold for binding other proteins dominates recent literature (3,(8)(9)(10). This view is reflected by the annotation of the HAT motif at InterPro, which states only that "the repeats may be involved in protein-protein interactions" (http://www.ebi.…”

mentioning

confidence: 63%

“…Mutations in Arabidopsis HCF107 cause defects in the translation and stabilization of mRNAs derived from the chloroplast psbH gene (6,15). Our results show that HCF107 binds ssRNA with specificity for sequences at the 5′ end of the processed psbH mRNA isoforms that require HCF107 for their accumulation.…”

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confidence: 66%

“…HCF107 is targeted to chloroplasts by an N-terminal transit peptide (6). Mature HCF107 (i.e., lacking the cleaved transit peptide) has 11 consecutive HAT motifs flanked by ∼100 aa on each side (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The HAT protein HCF107 stabilizes psbH mRNA, defines the processed psbH 5′ end, and enhances psbH translation in vivo (6,15). Analogous activities have been attributed to several members of the PPR family (reviewed in ref.…”

Section: Discussionmentioning

confidence: 99%

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RNA binding and RNA remodeling activities of the half-a-tetratricopeptide (HAT) protein HCF107 underlie its effects on gene expression

Hammani

Cook

Barkan

2012

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

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The half-a-tetratricopeptide repeat (HAT) motif is a helical repeat motif found in proteins that influence various aspects of RNA metabolism, including rRNA biogenesis, RNA splicing, and polyadenylation. This functional association with RNA suggested that HAT repeat tracts might bind RNA. However, RNA binding activity has not been reported for any HAT repeat tract, and recent literature has emphasized a protein binding role. In this study, we show that a chloroplast-localized HAT protein, HCF107, is a sequence-specific RNA binding protein. HCF107 consists of 11 tandem HAT repeats and short flanking regions that are also predicted to form helical hairpins. The minimal HCF107 binding site spans ∼11 nt, consistent with the possibility that HAT repeats bind RNA through a modular one repeat-1 nt mechanism. Binding of HCF107 to its native RNA ligand in the psbH 5′ UTR remodels local RNA structure and protects the adjacent RNA from exonucleases in vitro. These activities can account for the RNA stabilizing, RNA processing, and translational activation functions attributed to HCF107 based on genetic data. We suggest that analogous activities contribute to the functions of HAT domains found in ribonucleoprotein complexes in the nuclear-cytosolic compartment.helical repeat protein | plastid | pentatricopeptide repeat T he half-a-tetratricopeptide (HAT) motif is a helical repeat motif that has been functionally linked to RNA because of its presence exclusively in complexes that influence RNA metabolism (1). Examples of HAT domain proteins include Utp6, which is involved in nuclear pre-rRNA processing, Prp6, which is involved in nuclear pre-mRNA splicing, and CstF-77, which is involved in pre-mRNA cleavage and polyadenylation. The HAT motif is related to the tetratricopeptide repeat (TPR), a degenerate 34-aa motif that forms a pair of antiparallel α-helices (reviewed in ref.2). TPR motifs are typically found in tandem arrays, which stack to form a broad surface that binds protein ligands. Crystal structures of CstF-77 confirmed that HAT repeat tracts adopt a TPR-like structure (3, 4). The possibility that HAT repeat tracts might bind RNA has been suggested (1, 5-7), but the notion that HAT repeat tracts serve as a scaffold for binding other proteins dominates recent literature (3,(8)(9)(10)). This view is reflected by the annotation of the HAT motif at InterPro, which states only that "the repeats may be involved in protein-protein interactions" (http://www.ebi. ac.uk/interpro/IEntry?ac=IPR003107).Although TPR, HEAT, and several other helical repeat motifs form protein binding surfaces, similar structures have been shown to bind nucleic acids. Puf and pentatricopeptide repeat (PPR) motifs have been shown to bind RNA (reviewed in refs. 11 and 12), and mTERF, ALK, and TAL repeat motifs have been shown to bind DNA (reviewed in refs. 13 and 14). Thus, it seemed quite plausible that the presence of HAT domains exclusively in ribonucleoprotein complexes reflects the fact that HAT repeat tracts interact directly with RNA. In this ...

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confidence: 63%

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confidence: 66%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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RNA binding and RNA remodeling activities of the half-a-tetratricopeptide (HAT) protein HCF107 underlie its effects on gene expression

Hammani

Cook

Barkan

2012

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

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“…Indeed, we found the closest paralog of Mac1 in Chlamydomonas to be Mbb1, a TPR/HAT repeat protein involved in the stabilization or maturation of the psbB/T and psbH mRNAs (Vaistij et al, 2000a;Loizeau et al, 2014) (Supplemental Figure 3 and Supplemental Data Set 1). The ortholog of Mbb1 in vascular plants, HCF107, is required for the stability of psbH transcripts (Felder et al, 2001;Sane et al, 2005;Hammani et al, 2012).…”

Section: Identification Of Mac1mentioning

confidence: 99%

A Nucleus-Encoded Chloroplast Phosphoprotein Governs Expression of the Photosystem I Subunit PsaC in Chlamydomonas reinhardtii

Douchi

Longoni

et al. 2016

Plant Cell

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The nucleo-cytoplasmic compartment exerts anterograde control on chloroplast gene expression through numerous proteins that intervene at posttranscriptional steps. Here, we show that the maturation of psaC mutant (mac1) of Chlamydomonas reinhardtii is defective in photosystem I and fails to accumulate psaC mRNA. The MAC1 locus encodes a member of the Half-A-Tetratricopeptide (HAT) family of super-helical repeat proteins, some of which are involved in RNA transactions. The Mac1 protein localizes to the chloroplast in the soluble fraction. MAC1 acts through the 59 untranslated region of psaC transcripts and is required for their stability. Small RNAs that map to the 59end of psaC RNA in the wild type but not in the mac1 mutant are inferred to represent footprints of MAC1-dependent protein binding, and Mac1 expressed in bacteria binds RNA in vitro. A coordinate response to iron deficiency, which leads to dismantling of the photosynthetic electron transfer chain and in particular of photosystem I, also causes a decrease of Mac1. Overexpression of Mac1 leads to a parallel increase in psaC mRNA but not in PsaC protein, suggesting that Mac1 may be limiting for psaC mRNA accumulation but that other processes regulate protein accumulation. Furthermore, Mac 1 is differentially phosphorylated in response to iron availability and to conditions that alter the redox balance of the electron transfer chain.

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Translation and translational regulation in chloroplasts

Peled-Zehavi

Danon

2007

Topics in Current Genetics

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The nuclear gene HCF107 encodes a membrane‐associated R‐TPR (RNA tetratricopeptide repeat)‐containing protein involved in expression of the plastidial psbH gene in Arabidopsis

Cited by 65 publications

References 52 publications

RNA binding and RNA remodeling activities of the half-a-tetratricopeptide (HAT) protein HCF107 underlie its effects on gene expression

RNA binding and RNA remodeling activities of the half-a-tetratricopeptide (HAT) protein HCF107 underlie its effects on gene expression

A Nucleus-Encoded Chloroplast Phosphoprotein Governs Expression of the Photosystem I Subunit PsaC in Chlamydomonas reinhardtii

Translation and translational regulation in chloroplasts

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