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  1. Article: RNA-binding proteins: modular design for efficient function.

    Lunde, Bradley M / Moore, Claire / Varani, Gabriele

    Nature reviews. Molecular cell biology

    2007  Volume 8, Issue 6, Page(s) 479–490

    Abstract: Many RNA-binding proteins have modular structures and are composed of multiple repeats of just ... for many RNA-binding proteins, multiple modules define the fundamental structural unit that is responsible ... studies have investigated how different modules cooperate in regulating the RNA-binding specificity and ...

    Abstract Many RNA-binding proteins have modular structures and are composed of multiple repeats of just a few basic domains that are arranged in various ways to satisfy their diverse functional requirements. Recent studies have investigated how different modules cooperate in regulating the RNA-binding specificity and the biological activity of these proteins. They have also investigated how multiple modules cooperate with enzymatic domains to regulate the catalytic activity of enzymes that act on RNA. These studies have shown how, for many RNA-binding proteins, multiple modules define the fundamental structural unit that is responsible for biological function.
    MeSH term(s) Animals ; Catalytic Domain ; Dimerization ; Enzyme Activation ; Humans ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; RNA/chemistry ; RNA/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances RNA-Binding Proteins ; RNA (63231-63-0)
    Language English
    Publishing date 2007-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/nrm2178
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  2. Article ; Online: Engineered Protein Nanocages for Concurrent RNA and Protein Packaging In Vivo.

    Kwon, Seokmu / Giessen, Tobias W

    ACS synthetic biology

    2022  Volume 11, Issue 10, Page(s) 3504–3515

    Abstract: ... function by designing and characterizing encapsulins for concurrent RNA and protein encapsulation in vivo ... highly efficient and selective intrinsic protein packaging capabilities. Here, we expand encapsulin ... in vivo, are capable of efficient size-selective in vivo RNA packaging, can simultaneously load multiple ...

    Abstract Protein nanocages have emerged as an important engineering platform for biotechnological and biomedical applications. Among naturally occurring protein cages, encapsulin nanocompartments have recently gained prominence due to their favorable physico-chemical properties, ease of shell modification, and highly efficient and selective intrinsic protein packaging capabilities. Here, we expand encapsulin function by designing and characterizing encapsulins for concurrent RNA and protein encapsulation in vivo. Our strategy is based on modifying encapsulin shells with nucleic acid-binding peptides without disrupting the native protein packaging mechanism. We show that our engineered encapsulins reliably self-assemble in vivo, are capable of efficient size-selective in vivo RNA packaging, can simultaneously load multiple functional RNAs, and can be used for concurrent in vivo packaging of RNA and protein. Our engineered encapsulation platform has potential for codelivery of therapeutic RNAs and proteins to elicit synergistic effects and as a modular tool for other biotechnological applications.
    MeSH term(s) RNA/genetics ; Bacterial Proteins/genetics ; Peptides ; Biotechnology
    Chemical Substances RNA (63231-63-0) ; Bacterial Proteins ; Peptides
    Language English
    Publishing date 2022-09-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ISSN 2161-5063
    ISSN (online) 2161-5063
    DOI 10.1021/acssynbio.2c00391
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  3. Article: Control of CNS functions by RNA-binding proteins in neurological diseases.

    Zhou, Yijing / Dong, Fengping / Mao, Yingwei

    Current pharmacology reports

    2018  Volume 4, Issue 4, Page(s) 301–313

    Abstract: ... binding proteins (RBPs) that control neurological functions and pathogenesis in various neurodevelopmental and ... wide approaches revealed that many proteins associate with RNA, but do not contain any known RNA ... of neurological diseases. Insights into how RBPs modulate neural development are important for designing effective ...

    Abstract Purpose of review: This review summarizes recent studies on the molecular mechanisms of RNA binding proteins (RBPs) that control neurological functions and pathogenesis in various neurodevelopmental and neurodegenerative diseases, including autism spectrum disorders, schizophrenia, Alzheimer's disease, amyotrophic lateral sclerosis, frontotemporal dementia, and spinocerebellar ataxia.
    Recent findings: RBPs are critical players in gene expression that regulate every step of posttranscriptional modifications. Recent genome-wide approaches revealed that many proteins associate with RNA, but do not contain any known RNA binding motifs. Additionally, many causal and risk genes of neurodevelopmental and neurodegenerative diseases are RBPs. Development of high-throughput sequencing methods has mapped out the fingerprints of RBPs on transcripts and provides unprecedented potential to discover new mechanisms of neurological diseases. Insights into how RBPs modulate neural development are important for designing effective therapies for numerous neurodevelopmental and neurodegenerative diseases.
    Summary: RBPs have diverse mechanisms for modulating RNA processing and, thereby, controlling neurogenesis. Understanding the role of disease-associated RBPs in neurogenesis is vital for developing novel treatments for neurological diseases.
    Language English
    Publishing date 2018-05-02
    Publishing country Switzerland
    Document type Journal Article
    ISSN 2198-641X
    ISSN 2198-641X
    DOI 10.1007/s40495-018-0140-7
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  4. Article ; Online: Interfering with HuR-RNA Interaction: Design, Synthesis and Biological Characterization of Tanshinone Mimics as Novel, Effective HuR Inhibitors.

    Manzoni, Leonardo / Zucal, Chiara / Maio, Danilo Di / D'Agostino, Vito G / Thongon, Natthakan / Bonomo, Isabelle / Lal, Preet / Miceli, Marco / Baj, Vanessa / Brambilla, Marta / Cerofolini, Linda / Elezgarai, Saioa / Biasini, Emiliano / Luchinat, Claudio / Novellino, Ettore / Fragai, Marco / Marinelli, Luciana / Provenzani, Alessandro / Seneci, Pierfausto

    Journal of medicinal chemistry

    2018  Volume 61, Issue 4, Page(s) 1483–1498

    Abstract: The human antigen R (HuR) is an RNA-binding protein known to modulate the expression of target mRNA ... with its RNA substrate, thus imparing its function. Herein, inspired by DHTS structure, we designed and ... coding for proteins involved in inflammation, tumorigenesis, and stress responses and is a valuable ...

    Abstract The human antigen R (HuR) is an RNA-binding protein known to modulate the expression of target mRNA coding for proteins involved in inflammation, tumorigenesis, and stress responses and is a valuable drug target. We previously found that dihydrotanshinone-I (DHTS, 1) prevents the association of HuR with its RNA substrate, thus imparing its function. Herein, inspired by DHTS structure, we designed and synthesized an array of ortho-quinones (tanshinone mimics) using a function-oriented synthetic approach. Among others, compound 6a and 6n turned out to be more effective than 1, showing a nanomolar K
    MeSH term(s) Cell Line ; Diterpenes, Abietane ; Drug Design ; ELAV-Like Protein 1/metabolism ; Humans ; Molecular Dynamics Simulation ; Molecular Mimicry ; Protein Binding/drug effects ; Quinones/chemical synthesis ; Quinones/pharmacology ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Structure-Activity Relationship
    Chemical Substances Diterpenes, Abietane ; ELAV-Like Protein 1 ; Quinones ; RNA, Messenger ; RNA-Binding Proteins ; tanshinone (03UUH3J385)
    Language English
    Publishing date 2018-01-31
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.7b01176
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  5. Article: [Construction of CD36 gene silencing cell lines by lentivirus-mediated RNA interference and the effect on protein expression of caveolin-1].

    Li, Jingda / Yu, Chengjie / Wang, Renjun / Fu, Changzhen / Xiu, Zhilong / Liu, Qingping

    Sheng wu gong cheng xue bao = Chinese journal of biotechnology

    2018  Volume 34, Issue 1, Page(s) 110–121

    Abstract: ... by lentivirus-mediated RNA interference technique, and analyzed the effect of CD36 in caveolin-1 protein ... protein expression, demonstrating that CD36 modulates the caveolin-1 protein expression through the JNK ... in the gene silence cell line was 90%. Accompanied by a decrease in CD36 protein on cell surface, oxLDL binding ...

    Abstract CD36, the major scavenger receptor, is intimately involved in the uptake of oxLDL in macrophages. To further study the function of CD36 in macrophages, we constructed CD36 gene silence cell lines (J774A.1) by lentivirus-mediated RNA interference technique, and analyzed the effect of CD36 in caveolin-1 protein expression. At first, 5 shRNA fragments were designed and synthesized according to the coding sequence (CDS) region of CD36 gene. Next, the CD36-shRNA was inserted into lentiviral vector to yield pLKO.1-CD36-shRNA plasmid. After DNA sequencing, the pLKO.1-CD36-shRNA plasmid and psiCHECK-II-CD36 were co-transfected into the 293T cells to screen the efficient CD36-shRNA. The efficient CD36-shRNA plasmid and the helper plasmid were co-transfected into the 293T cells to package the lentivirus, and then infected the J774A.1 cells. After screening by puromycin, CD36 gene silence cell lines (J774A.1) was established. Western blotting and confocal fluorescence microscopy results showed that the CD36 silencing efficiency in the gene silence cell line was 90%. Accompanied by a decrease in CD36 protein on cell surface, oxLDL binding to CD36 was significantly inhibited, indicating that the CD36 gene silence cell line is successfully established. Finally, the oxLDL stimulation and inhibitor experiments results showed that the CD36 knockdown significantly suppresses the phosphorylation of JNK and ERK, thereby inhibiting the oxLDL-induced caveolin-1 protein expression, demonstrating that CD36 modulates the caveolin-1 protein expression through the JNK/ERK-mediated signaling transduction.
    MeSH term(s) Animals ; CD36 Antigens/genetics ; Caveolin 1/metabolism ; Cell Line ; Genetic Vectors ; Lentivirus ; Mice ; RNA Interference ; RNA, Small Interfering ; Signal Transduction
    Chemical Substances CD36 Antigens ; Caveolin 1 ; RNA, Small Interfering
    Language Chinese
    Publishing date 2018-01-30
    Publishing country China
    Document type Journal Article
    ZDB-ID 1042206-7
    ISSN 1000-3061 ; 1042-749X
    ISSN 1000-3061 ; 1042-749X
    DOI 10.13345/j.cjb.170135
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  6. Article ; Online: Three-dimensionally designed protein-responsive RNA devices for cell signaling regulation.

    Kashida, Shunnichi / Inoue, Tan / Saito, Hirohide

    Nucleic acids research

    2012  Volume 40, Issue 18, Page(s) 9369–9378

    Abstract: ... converters designed to bind to the target U1A or nuclear factor-κB (NF-κB) p50 proteins expressed in human ... efficient molecular devices that function in living cells. Here, we demonstrate a 3D structure-based ... by modulating the function of the RNA-processing enzyme Dicer. The inhibitory effect on Dicer cleavage against ...

    Abstract The three-dimensional (3D) structures of many biomacromolecules have been solved to reveal the functions of these molecules. However, these 3D structures have rarely been applied to constructing efficient molecular devices that function in living cells. Here, we demonstrate a 3D structure-based molecular design principle for constructing short hairpin RNA (shRNA)-mediated genetic information converters; these converters respond to specific proteins and trigger the desired gene expression by modulating the function of the RNA-processing enzyme Dicer. The inhibitory effect on Dicer cleavage against the shRNA designed to specifically bind to U1A spliceosomal protein was correlated with the degree of steric hindrance between Dicer and the shRNA-protein complex in vitro: The level of the hindrance was predicted based on the models. Moreover, the regulation of gene expression was achieved by using the shRNA converters designed to bind to the target U1A or nuclear factor-κB (NF-κB) p50 proteins expressed in human cells. The 3D molecular design approach is widely applicable for developing new devices in synthetic biology.
    MeSH term(s) Animals ; Cells, Cultured ; Humans ; Imaging, Three-Dimensional ; Mice ; Models, Molecular ; NF-kappa B p50 Subunit/metabolism ; Nucleotide Motifs ; RNA Interference ; RNA, Small Interfering/chemistry ; RNA, Small Interfering/metabolism ; Ribonuclease III/chemistry ; Ribonuclease III/metabolism ; Ribonucleoprotein, U1 Small Nuclear/chemistry ; Ribonucleoprotein, U1 Small Nuclear/genetics ; Ribonucleoprotein, U1 Small Nuclear/metabolism ; Signal Transduction
    Chemical Substances NF-kappa B p50 Subunit ; RNA, Small Interfering ; Ribonucleoprotein, U1 Small Nuclear ; U1A protein ; Ribonuclease III (EC 3.1.26.3)
    Language English
    Publishing date 2012-07-18
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gks668
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  7. Article: The GTP binding sites interacted with RNA-dependent RNA polymerase of classical swine fever virus in de novo initiation.

    Xu, Zhuofei / Chao, Yanjie / Si, Youhui / Wang, Jian / Jin, Meilin / Guo, Aizhen / Qian, Ping / Zhou, Rui / Chen, Huanchun

    In silico biology

    2008  Volume 8, Issue 1, Page(s) 21–32

    Abstract: The NS5B protein of classical swine fever virus (CSFV) is an important enzyme bearing a unique RNA ... unclearly described at present. Our aim is to reveal the RdRp-GTP docking sites and the effective modules ... GTP binding pocket of the polymerase was pointed out: five residues E227, S408, R427, K435, and R439 ...

    Abstract The NS5B protein of classical swine fever virus (CSFV) is an important enzyme bearing a unique RNA-dependent RNA polymerase (RdRp) activity. The RdRp plays a crucial role in the viral replication cycle and in forming a replicase complex. However, the initiating synthesis mechanism of the CSFV RNA polymerase is unclearly described at present. Our aim is to reveal the RdRp-GTP docking sites and the effective modules of GTP initially bound to the polymerase in starting initiation of replication according to a well predicted CSFV RdRp model. Based on some known crystal structures of RNA polymerase, computational methods were used to establish the model of a CSFV RdRp. An analogous mechanism of CSFV RNA polymerase in de novo initiation was subsequently represented through docking a GTP into the structure model. The unique GTP binding pocket of the polymerase was pointed out: five residues E227, S408, R427, K435, and R439 involved in steady hydrogen bonds and two residues C407 and L232 involved in hydrophobic contact with the GTP. From a genetic evolutionary point of view, three residues C407, S408 and R427 have been suggested to be of particular importance by analysis of residue conservation. It is suggested that these crucial residues should have very significant function in the de novo initiation of the rigorous CSFV polymerase model, which can lead us to design experiments for studying the mechanism of viral replication and develop valid anti-viral drugs.
    MeSH term(s) Amino Acid Sequence ; Binding Sites ; Classical swine fever virus/enzymology ; Classical swine fever virus/genetics ; Guanosine Triphosphate/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; RNA Replicase/chemistry ; RNA Replicase/genetics ; RNA Replicase/metabolism ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Sequence Homology, Amino Acid ; Virus Replication
    Chemical Substances RNA, Viral ; Guanosine Triphosphate (86-01-1) ; RNA Replicase (EC 2.7.7.48)
    Language English
    Publishing date 2008
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2084578-9
    ISSN 1386-6338
    ISSN 1386-6338
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    Zs.A 5988: Show issues Location:
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  8. Article ; Online: Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear export.

    Brockmann, Christoph / Soucek, Sharon / Kuhlmann, Sonja I / Mills-Lujan, Katherine / Kelly, Seth M / Yang, Ji-Chun / Iglesias, Nahid / Stutz, Francoise / Corbett, Anita H / Neuhaus, David / Stewart, Murray

    Structure (London, England : 1993)

    2012  Volume 20, Issue 6, Page(s) 1007–1018

    Abstract: ... the polyadenosine-RNA-binding protein, Nab2, which contains seven CCCH Zn fingers. We describe here the solution ... structure of fingers 5-7, which are necessary and sufficient for high-affinity polyadenosine-RNA binding ... coherence is lost in the RNA-binding compromised Nab2-C437S mutant, which also suppresses the rat8-2 allele ...

    Abstract Polyadenylation regulation and efficient nuclear export of mature mRNPs both require the polyadenosine-RNA-binding protein, Nab2, which contains seven CCCH Zn fingers. We describe here the solution structure of fingers 5-7, which are necessary and sufficient for high-affinity polyadenosine-RNA binding, and identify key residues involved. These Zn fingers form a single structural unit. Structural coherence is lost in the RNA-binding compromised Nab2-C437S mutant, which also suppresses the rat8-2 allele of RNA helicase Dbp5. Structure-guided Nab2 variants indicate that dbp5(rat8-2) suppression is more closely linked to hyperadenylation and suppression of mutant alleles of the nuclear RNA export adaptor, Yra1, than to affinity for polyadenosine-RNA. These results indicate that, in addition to modulating polyA tail length, Nab2 has an unanticipated function associated with generating export-competent mRNPs, and that changes within fingers 5-7 lead to suboptimal assembly of mRNP export complexes that are more easily disassembled by Dbp5 upon reaching the cytoplasm.
    MeSH term(s) Active Transport, Cell Nucleus ; Adenosine/chemistry ; Amino Acid Sequence ; Amino Acid Substitution ; Conserved Sequence ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nuclear Magnetic Resonance, Biomolecular ; Nucleocytoplasmic Transport Proteins/chemistry ; Nucleocytoplasmic Transport Proteins/genetics ; Nucleocytoplasmic Transport Proteins/metabolism ; Polymers/chemistry ; Protein Binding ; Protein Structure, Tertiary ; RNA Transport ; RNA, Messenger/chemistry ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Surface Properties ; Thermodynamics ; Zinc Fingers
    Chemical Substances NAB2 protein, S cerevisiae ; Nucleocytoplasmic Transport Proteins ; Polymers ; RNA, Messenger ; RNA-Binding Proteins ; Saccharomyces cerevisiae Proteins ; polyadenosine (30143-02-3) ; Adenosine (K72T3FS567)
    Language English
    Publishing date 2012-05-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2012.03.011
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  9. Article: RNA aptamers directed to discrete functional sites on a single protein structural domain.

    Shi, Hua / Fan, Xiaochun / Sevilimedu, Aarti / Lis, John T

    Proceedings of the National Academy of Sciences of the United States of America

    2007  Volume 104, Issue 10, Page(s) 3742–3746

    Abstract: ... by generating aptamers directed to discrete functional surfaces of the yeast TATA-binding protein (TBP ... innovative approaches to modulating other highly connected regulatory proteins. ... whereas a few proteins have many. These densely connected protein "hubs" are critical for the system-wide behavior ...

    Abstract Cellular regulatory networks are organized such that many proteins have few interactions, whereas a few proteins have many. These densely connected protein "hubs" are critical for the system-wide behavior of cells, and the capability of selectively perturbing a subset of interactions at these hubs is invaluable in deciphering and manipulating regulatory mechanisms. SELEX-generated RNA aptamers are proving to be highly effective reagents for inhibiting targeted proteins, but conventional methods generate one or several aptamer clones that usually bind to a single target site most preferred by a nucleic acid ligand. We advance a generalized scheme for isolating aptamers to multiple sites on a target molecule by reducing the ability of the preferred site to select its cognate aptamer. We demonstrate the use of this scheme by generating aptamers directed to discrete functional surfaces of the yeast TATA-binding protein (TBP). Previously we selected "class 1" RNA aptamers that interfere with the TBP's binding to TATA-DNA. By masking TBP with TATA-DNA or an unamplifiable class 1 aptamer, we isolated a new aptamer class, "class 2," that can bind a TBP.DNA complex and is in competition with binding another general transcription factor, TFIIA. Moreover, we show that both of these aptamers inhibit RNA polymerase II-dependent transcription, but analysis of template-bound factors shows they do so in mechanistically distinct and unexpected ways that can be attributed to binding either the DNA or TFIIA recognition sites. These results should spur innovative approaches to modulating other highly connected regulatory proteins.
    MeSH term(s) Aptamers, Nucleotide/chemistry ; Aptamers, Nucleotide/genetics ; Base Sequence ; Binding Sites ; Evolution, Molecular ; Fungal Proteins/chemistry ; Models, Molecular ; Molecular Conformation ; Molecular Sequence Data ; Nucleic Acids/chemistry ; Polymers/chemistry ; Protein Conformation ; Protein Structure, Tertiary ; RNA/chemistry ; TATA-Box Binding Protein/chemistry ; Transcription Factor TFIIA/chemistry
    Chemical Substances Aptamers, Nucleotide ; Fungal Proteins ; Nucleic Acids ; Polymers ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; RNA (63231-63-0)
    Language English
    Publishing date 2007-02-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0607805104
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  10. Article ; Online: Synthetic RNA modules for fine-tuning gene expression levels in yeast by modulating RNase III activity.

    Babiskin, Andrew H / Smolke, Christina D

    Nucleic acids research

    2011  Volume 39, Issue 19, Page(s) 8651–8664

    Abstract: ... modulate cleavage rates, providing a modular assembly strategy for this class of RNA-based control elements. ... The design of synthetic gene networks requires an extensive genetic toolbox to control ... of RNA-based control modules, which act through post-transcriptional processing of transcripts ...

    Abstract The design of synthetic gene networks requires an extensive genetic toolbox to control the activities and levels of protein components to achieve desired cellular functions. Recently, a novel class of RNA-based control modules, which act through post-transcriptional processing of transcripts by directed RNase III (Rnt1p) cleavage, were shown to provide predictable control over gene expression and unique properties for manipulating biological networks. Here, we increase the regulatory range of the Rnt1p control elements, by modifying a critical region for enzyme binding to its hairpin substrates, the binding stability box (BSB). We used a high throughput, cell-based selection strategy to screen a BSB library for sequences that exhibit low fluorescence and thus high Rnt1p processing efficiencies. Sixteen unique BSBs were identified that cover a range of protein expression levels, due to the ability of the sequences to affect the hairpin cleavage rate and to form active cleavable complexes with Rnt1p. We further demonstrated that the activity of synthetic Rnt1p hairpins can be rationally programmed by combining the synthetic BSBs with a set of sequences located within a different region of the hairpin that directly modulate cleavage rates, providing a modular assembly strategy for this class of RNA-based control elements.
    MeSH term(s) Gene Expression Regulation, Fungal ; Gene Library ; High-Throughput Screening Assays ; RNA/chemistry ; RNA/metabolism ; Regulatory Sequences, Ribonucleic Acid ; Ribonuclease III/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Regulatory Sequences, Ribonucleic Acid ; Saccharomyces cerevisiae Proteins ; RNA (63231-63-0) ; RNT1 protein, S cerevisiae (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3)
    Language English
    Publishing date 2011-07-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkr445
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