scholarly journals Independent evolution of tetraloop in enterovirus oriL replicative element and its putative binding partners in virus protein 3C

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3896 ◽  
Author(s):  
Maria A. Prostova ◽  
Andrei A. Deviatkin ◽  
Irina O. Tcelykh ◽  
Alexander N. Lukashev ◽  
Anatoly P. Gmyl
Keyword(s):  
Amino Acid ◽  
Genome Stability ◽  
Rna Binding ◽  
Virus Protein ◽  
Apical Region ◽  
Reading Frame ◽  
Loop Region ◽  
Binding Partners ◽  
D Loop ◽  
Species Specific

BackgroundEnteroviruses are small non-enveloped viruses with a (+) ssRNA genome with one open reading frame. Enterovirus protein 3C (or 3CD for some species) binds the replicative element oriL to initiate replication. The replication of enteroviruses features a low-fidelity process, which allows the virus to adapt to the changing environment on the one hand, and requires additional mechanisms to maintain the genome stability on the other. Structural disturbances in the apical region of oriL domain d can be compensated by amino acid substitutions in positions 154 or 156 of 3C (amino acid numeration corresponds to poliovirus 3C), thus suggesting the co-evolution of these interacting sequences in nature. The aim of this work was to understand co-evolution patterns of two interacting replication machinery elements in enteroviruses, the apical region of oriL domain d and its putative binding partners in the 3C protein.MethodsTo evaluate the variability of the domain d loop sequence we retrieved all available full enterovirus sequences (>6, 400 nucleotides), which were present in the NCBI database on February 2017 and analysed the variety and abundance of sequences in domain d of the replicative element oriL and in the protein 3C.ResultsA total of 2,842 full genome sequences was analysed. The majority of domain d apical loops were tetraloops, which belonged to consensus YNHG (Y = U/C, N = any nucleotide, H = A/C/U). The putative RNA-binding tripeptide 154–156 (Enterovirus C3C protein numeration) was less diverse than the apical domain d loop region and, in contrast to it, was species-specific.DiscussionDespite the suggestion that the RNA-binding tripeptide interacts with the apical region of domain d, they evolve independently in nature. Together, our data indicate the plastic evolution of both interplayers of 3C-oriL recognition.

scholarly journals Independent evolution of tetraloop in enterovirus oriL replicative element and its putative binding partners in protein 3C

2017 ◽  
Author(s):  
Maria A Prostova ◽  
Andrei A Deviatkin ◽  
Irina O Tcelykh ◽  
Alexander N Lukashev ◽  
Anatoly P Gmyl
Keyword(s):  
Amino Acid ◽  
Genome Stability ◽  
Rna Binding ◽  
Apical Region ◽  
Reading Frame ◽  
Loop Region ◽  
Binding Partners ◽  
D Loop ◽  
The One ◽  
Species Specific

Background. Enteroviruses are small non-enveloped viruses with (+) ssRNA genome with one open reading frame. Enterovirus protein 3C (or 3CD for some species) binds the replicative element oriL to initiate replication. The replication of enteroviruses features low fidelity, which allows the virus to adapt to the changing environment on the one hand, and requires additional mechanisms to maintain the genome stability on the other. Structural disturbances in the apical region of oriL domain d can be compensated by amino acid substitutions in positions 154 or 156 of 3C (amino acid numeration corresponds to poliovirus 3C), thus suggesting the co-evolution of these interacting sequences in nature. The aim of this work was to understand co-evolution patterns of two interacting replication machinery elements in enteroviruses, the apical region of oriL domain d and its putative binding partners in the 3C protein. Methods.To evaluate the variability of the domain d loop sequence we retrieved all available full enterovirus sequences (>6400 nucleotides), which were present in the NCBI database on February 2017 and analysed the variety and abundance of sequences in domain d of the replicative element oriL and in the protein 3C. Results.A total of 2,842 full genome sequences was analysed. The majority of domain d apical loops were tetraloops, which belonged to consensus YNHG (Y=U/C, N=any nucleotide, H=A/C/U). The putative RNA-binding tripeptide 154-156 (Enterovirus C 3C protein numeration) was less diverse than the apical domain d loop region and, in contrast to it, was species-specific. Discussion. Despite the suggestion that the RNA-binding tripeptide interacts with the apical region of domain d, they evolve independently in nature. Together, our data indicate the plastic evolution of both interplayers of 3C-oriL recognition.

scholarly journals Independent evolution of tetraloop in enterovirus oriL replicative element and its putative binding partners in protein 3C

2017 ◽  
Author(s):  
Maria A Prostova ◽  
Andrei A Deviatkin ◽  
Irina O Tcelykh ◽  
Alexander N Lukashev ◽  
Anatoly P Gmyl
Keyword(s):  
Amino Acid ◽  
Genome Stability ◽  
Rna Binding ◽  
Apical Region ◽  
Reading Frame ◽  
Loop Region ◽  
Binding Partners ◽  
D Loop ◽  
The One ◽  
Species Specific

Background. Enteroviruses are small non-enveloped viruses with (+) ssRNA genome with one open reading frame. Enterovirus protein 3C (or 3CD for some species) binds the replicative element oriL to initiate replication. The replication of enteroviruses features low fidelity, which allows the virus to adapt to the changing environment on the one hand, and requires additional mechanisms to maintain the genome stability on the other. Structural disturbances in the apical region of oriL domain d can be compensated by amino acid substitutions in positions 154 or 156 of 3C (amino acid numeration corresponds to poliovirus 3C), thus suggesting the co-evolution of these interacting sequences in nature. The aim of this work was to understand co-evolution patterns of two interacting replication machinery elements in enteroviruses, the apical region of oriL domain d and its putative binding partners in the 3C protein. Methods.To evaluate the variability of the domain d loop sequence we retrieved all available full enterovirus sequences (>6400 nucleotides), which were present in the NCBI database on February 2017 and analysed the variety and abundance of sequences in domain d of the replicative element oriL and in the protein 3C. Results.A total of 2,842 full genome sequences was analysed. The majority of domain d apical loops were tetraloops, which belonged to consensus YNHG (Y=U/C, N=any nucleotide, H=A/C/U). The putative RNA-binding tripeptide 154-156 (Enterovirus C 3C protein numeration) was less diverse than the apical domain d loop region and, in contrast to it, was species-specific. Discussion. Despite the suggestion that the RNA-binding tripeptide interacts with the apical region of domain d, they evolve independently in nature. Together, our data indicate the plastic evolution of both interplayers of 3C-oriL recognition.

scholarly journals Independent evolution of tetraloop in enterovirus oriL replicative element and its putative binding partners in protein 3C

2017 ◽  
Author(s):  
Maria A Prostova ◽  
Andrey A Deviatkin ◽  
Irina O Tcelykh ◽  
Alexander N Lukashev ◽  
Anatoly P Gmyl
Keyword(s):  
Amino Acid ◽  
Genome Stability ◽  
Rna Binding ◽  
Apical Region ◽  
Reading Frame ◽  
Loop Region ◽  
Binding Partners ◽  
D Loop ◽  
The One ◽  
Species Specific

Background. Enteroviruses are small non-enveloped viruses with (+) ssRNA genome with one open reading frame. Enterovirus protein 3C (or 3CD for some species) binds replicative element oriL to initiate replication. The replication of enteroviruses features low fidelity that allows virus to adapt to changing environment on the one hand, and requires additional mechanisms to maintain the genome stability on the other. Structural disturbances in the apical region of oriL domain d can be compensated by amino acid substitutions in positions 154 or 156 of 3C (amino acid numeration corresponds to poliovirus 3C), thus suggesting co-evolution of these interacting sequences in nature. The aim of this work was to understand co-evolution patterns of two interacting replication machinery elements in enteroviruses, the apical region of oriL domain d and its putative binding partners in the 3C protein. Methods.To evaluate the variability of the domain d loop sequence we retrieved all available full enterovirus sequences (>6400 nucleotides) that were present in the NCBI database on February 2017 and analyzed variety and abundance of sequences in domain d of replicative element oriL and in the protein 3C. Results. A total of 2842 full genome sequences were analyzed. Majority of domain d apical loops were tetraloops, which belonged to consensus YNHG (Y=U/C, N=any nucleotide, H=A/C/U). Putative RNA-binding tripeptide 154-156 (Enterovirus C 3C protein numeration) was less diverse than the apical domain d loop region and, in contrast to it, was species-specific. Discussion. Despite RNA-binding tripeptide is suggested to interact with apical region of domain d, they evolve independently in nature. Together, our data indicates plastic evolution of both interplayers of 3C-oriL recognition.

scholarly journals Sequence and structure of mtr, an amino acid transport gene of Neurospora crassa

Genome ◽  
1991 ◽  
Vol 34 (4) ◽  
pp. 644-651 ◽  
Author(s):  
Kenneth Koo ◽  
W. Dorsey Stuart
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Neurospora Crassa ◽  
Rna Binding ◽  
Signal Sequence ◽  
Average Length ◽  
Open Reading Frame ◽  
Mrna Transcript ◽  
S1 Nuclease ◽  
Reading Frame

The gene product of the mtr locus of Neurospora crassa is required for the transport of neutral aliphatic and aromatic amino acids via the N system. We have previously cloned three cosmids containing Neurospora DNA that complement the mtr-6(r) mutant allele. The cloned DNAs were tightly linked to restriction fragment length polymorphisms that flank the mtr locus. A 2.9-kbp fragment from one cosmid was subcloned and found to complement the mtr-6(r) allele. Here we report the sequence of the fragment that hybridized to a poly(A)+ mRNA transcript of about 2300 nucleotides. We have identified an 845-bp open reading frame (ORF) having a 59-bp intron as the potential mtr ORF. S1 nuclease analysis of the transcript confirmed the transcript size and the presence of the intron. A second open reading frame was found upstream in the same reading frame as the mtr ORF and appears to be present in the mRNA transcript. The mtr ORF is predicted to encode a 261 amino acid polypeptide with a molecular mass of 28 613 Da. The proposed polypeptide exhibits six potential α-helical transmembrane domains with an average length of 23 amino acids, does not have a signal sequence, and contains amino acid sequence homologous to an RNA binding motif.Key words: sequence, membranes, ribonucleoprotein.

scholarly journals Identification of Girella punctata and G. leonina by PCR-RFLP analysis

2006 ◽  
Vol 64 (2) ◽  
pp. 328-331 ◽  
Author(s):  
Shiro Itoi ◽  
Takashi Saito ◽  
Mai Shimojo ◽  
Sayaka Washio ◽  
Haruo Sugita
Keyword(s):  
Rflp Analysis ◽  
Morphological Identification ◽  
Similar Species ◽  
Sequencing Analysis ◽  
Electrophoretic Patterns ◽  
Loop Region ◽  
Site Mapping ◽  
Pcr Rflp ◽  
D Loop ◽  
Species Specific

Abstract Itoi, S., Saito, T., Shimojo, M., Washio, S., and Sugita, H. 2007. Identification of Girella punctata and G. leonina by PCR-RFLP analysis. – ICES Journal of Marine Science, 64: 328–331. Two Girella species, Girella punctata and G. leonina, are sympatric sister species with an extensive overlap in their respective distributions on shallow rocky reefs from Hong Kong to the south of the Japanese Islands. Juveniles of the two species cannot be discriminated easily on the basis of external characters. In this study, after morphological identification of the species, sequencing analysis was carried out for the partial 16S ribosomal RNA gene and for the D-loop region in mitochondrial DNA. A total of 109 specimens was examined. Restriction site mapping of the sequences suggested that the electrophoretic patterns of polymerase chain reaction (PCR)-based restriction fragment length polymorphism (RFLP) analysis of the gene products would produce a species-specific banding pattern. Subsequently, the PCR-RFLP analysis showed that the method was as effective for separating the two morphologically similar species of the genus Girella as the sequencing analysis.

scholarly journals MAC5, an RNA-binding protein, protects pri-miRNAs from SERRATE-dependent exoribonuclease activities

2020 ◽  
Vol 117 (38) ◽  
pp. 23982-23990 ◽  
Author(s):  
Shengjun Li ◽  
Mu Li ◽  
Kan Liu ◽  
Huimin Zhang ◽  
Shuxin Zhang ◽  
...  
Keyword(s):  
Rna Binding ◽  
Rna Binding Protein ◽  
Dual Role ◽  
Mirna Biogenesis ◽  
Core Component ◽  
Stem Loop ◽  
Loop Region ◽  
Nuclear Rna ◽  
Efficient Processing ◽  
The Stability

MAC5 is a component of the conserved MOS4-associated complex. It plays critical roles in development and immunity. Here we report that MAC5 is required for microRNA (miRNA) biogenesis. MAC5 interacts with Serrate (SE), which is a core component of the microprocessor that processes primary miRNA transcripts (pri-miRNAs) into miRNAs and binds the stem-loop region of pri-miRNAs. MAC5 is essential for both the efficient processing and the stability of pri-miRNAs. Interestingly, the reduction of pri-miRNA levels inmac5is partially caused by XRN2/XRN3, the nuclear-localized 5′-to-3′ exoribonucleases, and depends on SE. These results reveal that MAC5 plays a dual role in promoting pri-miRNA processing and stability through its interaction with SE and/or pri-miRNAs. This study also uncovers that pri-miRNAs need to be protected from nuclear RNA decay machinery, which is connected to the microprocessor.

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