An rpoB signature sequence provides unique resolution for the molecular typing of cyanobacteria

The use of morphological characters for the classification of cyanobacteria has often led to ambiguous strain assignment. In the past two decades, the availability of sequences, such as those of the 16S rRNA, nif, cpc and rpoC1 genes, and the use of metagenomics, has steadily increased and has made the reconstruction of evolutionary relationships of some cyanobacterial groups possible in addition to improving strain assignment. Conserved indels (insertions/deletions) are present in all cyanobacterial RpoB (β subunit of RNA polymerase) sequences presently available in public databases. These indels are located in the Rpb2_6 domain of RpoB, which is involved in DNA binding and DNA-directed RNA polymerase activity. They are variable in length (6–44 aa) and sequence, and form part of what appears to be a longer signature sequence (43–81 aa). Indeed, a number of these sequences turn out to be distinctive among several strains of a given genus and even among strains of a given species. These signature sequences can thus be used to identify cyanobacteria at a subgenus level and can be useful molecular markers to establish the taxonomic positions of cyanobacterial isolates in laboratory cultures, and/or to assess cyanobacterial biodiversity in space and time in natural ecosystems.

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Changes in RNA polymerase activity in isolated mouse uterine nuclei during the decidual cell reaction

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis ◽

10.1016/0005-2787(78)90269-1 ◽

1978 ◽

Vol 521 (1) ◽

pp. 267-273 ◽

Cited By ~ 2

Author(s):

M.J. Serra ◽

B.E. Ledford ◽

J.C. Rankin ◽

B. Baggett

Keyword(s):

Rna Polymerase ◽

Polymerase Activity ◽

Decidual Cell ◽

Cell Reaction ◽

Rna Polymerase Activity

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Functional analysis of influenza rna polymerase activity by the use of caps, oligonucleotides and polynucleotides

Antiviral Research ◽

10.1016/0166-3542(81)90036-x ◽

1981 ◽

Vol 1 (2) ◽

pp. 97-105 ◽

Cited By ~ 8

Author(s):

S. Stridh ◽

B. Öberg ◽

J. Chattopadhyaya ◽

S. Josephson

Keyword(s):

Functional Analysis ◽

Rna Polymerase ◽

Polymerase Activity ◽

Rna Polymerase Activity

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Pharmaceutical interference of the EWS-FLI1-driven transcriptome by co-targeting H3K27ac and RNA polymerase activity in Ewing Sarcoma

Molecular Cancer Therapeutics ◽

10.1158/1535-7163.mct-20-0489 ◽

2021 ◽

pp. molcanther.MCT-20-0489-A.2020

Author(s):

Daniel A. R. Heisey ◽

Sheeba Jacob ◽

Timonthy L Lochmann ◽

Richard Kurupi ◽

Maninderjit S. Ghotra ◽

...

Keyword(s):

Rna Polymerase ◽

Ewing Sarcoma ◽

Polymerase Activity ◽

Rna Polymerase Activity

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RNA polymerase activity in virions from Ustilago maydis

Molecular and Cellular Biology ◽

10.1128/mcb.4.1.188-194.1984 ◽

1984 ◽

Vol 4 (1) ◽

pp. 188-194

Author(s):

B S Ben-Tzvi ◽

Y Koltin ◽

M Mevarech ◽

A Tamarkin

Keyword(s):

Rna Polymerase ◽

Viral Genome ◽

Ustilago Maydis ◽

Polymerase Activity ◽

Reaction Products ◽

Double Stranded Rna ◽

Rna Molecules ◽

Rna Transcripts ◽

Rna Polymerase Activity

RNA polymerase activity is associated with the double-stranded RNA virions of Ustilago maydis. The reaction products of the polymerase activity are single-stranded RNA molecules. The RNA molecules synthesized are homologous to the three classes of double-stranded RNA molecules that typify the viral genome. The single-stranded RNA synthesized is released from the virions. The molecular weight of the single-stranded RNA transcripts is about half the size of the double-stranded RNA segments, and thus, it appears that in the in vitro reaction, full-length transcripts can be obtained.

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HDAC6 Restricts Influenza A Virus by Deacetylation of the RNA Polymerase PA Subunit

Journal of Virology ◽

10.1128/jvi.01896-18 ◽

2018 ◽

Vol 93 (4) ◽

Cited By ~ 12

Author(s):

Huan Chen ◽

Yingjuan Qian ◽

Xin Chen ◽

Zhiyang Ruan ◽

Yuetian Ye ◽

...

Keyword(s):

Life Cycle ◽

Rna Polymerase ◽

Influenza A Virus ◽

Influenza A ◽

Molecular Mechanisms ◽

Polymerase Activity ◽

Negative Regulator ◽

Host Protein ◽

Spectrometric Analysis ◽

Rna Polymerase Activity

ABSTRACT The life cycle of influenza A virus (IAV) is modulated by various cellular host factors. Although previous studies indicated that IAV infection is controlled by HDAC6, the deacetylase involved in the regulation of PA remained unknown. Here, we demonstrate that HDAC6 acts as a negative regulator of IAV infection by destabilizing PA. HDAC6 binds to and deacetylates PA, thereby promoting the proteasomal degradation of PA. Based on mass spectrometric analysis, Lys(664) of PA can be deacetylated by HDAC6, and the residue is crucial for PA protein stability. The deacetylase activity of HDAC6 is required for anti-IAV activity, because IAV infection was enhanced due to elevated IAV RNA polymerase activity upon HDAC6 depletion and an HDAC6 deacetylase dead mutant (HDAC6-DM; H216A, H611A). Finally, we also demonstrate that overexpression of HDAC6 suppresses IAV RNA polymerase activity, but HDAC6-DM does not. Taken together, our findings provide initial evidence that HDAC6 plays a negative role in IAV RNA polymerase activity by deacetylating PA and thus restricts IAV RNA transcription and replication. IMPORTANCE Influenza A virus (IAV) continues to threaten global public health due to drug resistance and the emergence of frequently mutated strains. Thus, it is critical to find new strategies to control IAV infection. Here, we discover one host protein, HDAC6, that can inhibit viral RNA polymerase activity by deacetylating PA and thus suppresses virus RNA replication and transcription. Previously, it was reported that IAV can utilize the HDAC6-dependent aggresome formation mechanism to promote virus uncoating, but HDAC6-mediated deacetylation of α-tubulin inhibits viral protein trafficking at late stages of the virus life cycle. These findings together will contribute to a better understanding of the role of HDAC6 in regulating IAV infection. Understanding the molecular mechanisms of HDAC6 at various periods of viral infection may illuminate novel strategies for developing antiviral drugs.

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