Together, these mechanisms are known as attenuation and antitermination, and both involve controlling the formation of a transcription. Some antitermination factors allow bypass of a single terminator in response to a . Attenuation through ribosome positioning, Leader RNA, Typical of amino. This mechanism is very similar to attenuation, but antitermination can be distinguished RNA-Binding Protein-Mediated Antitermination: The Sac/Bgl Family of.

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It was proposed that such a complex under inducing conditions would prevent ribosome release 35reminiscent of characterized translation attenuation mechanisms Once the translating ribosome reaches the UGA stop codon, ribosome release exposes a rut Rho utilization site that immediately follows the stop codon.

Stalled ribosome occludes rut or hinders Rho—NusG interactions. NusA can stimulate Q activity. Belogurov GA, et al. When functional, expression of this operon is regulated by antitermination mediated by the BglG protein in response to the levels of b-glucosides 4.

These ligands bind to their RNA targets with high affinity and selectivity in the absence of accessory proteins 59 — The majority of known antitermination mechanisms are passive TABLE 1 and are specific for intrinsic terminators, in part because these signals are simple and induce termination at antitermniation defined position. An additional factor or factors that can be supplied by a cellular extract are required, but their identities are unknown.

Structural classification of bacterial response regulators: Ruiz and the anonymous referees for their help in improving the manuscript. A combination of approaches and analysis of diverse termination signals will be required to identify the features that dictate the preferred termination pathway at each site.


A regulatory RNA required for antitermination of biofilm and capsular polysaccharide operons in Bacillales. Another important conserved feature of the leader region of these genes is the presence of a triplet sequence corresponding to a codon for the appropriate amino acid for each operon. To understand termination and its control by accessory factors, we must now probe the structure and dynamics of termination intermediates in real time.

LicT regulates antiterminattion licS gene, which is involved in b-glucan utilization in B.

The antitermination protein pN acts specifically on the immediate early transcription units. There are three mechanisms by which an antiterminator can act on RNA: It is used at two stages of phage expression. When cells are growing with inducing levels of tryptophan, TnaC, or a complex of TnaC with an unidentified protein, prevents ribosome release at the tnaC stop codon, thereby masking the rut site and, hence, blocking Rho interaction with the transcript. Control of the Bacillus subtilis attennuation protein GlcT by phosphorylation.

Antitermination Control of Gene Expression (Molecular Biology)

The role of NusG in the N antitermination reaction is not clear. The carboxy-terminal domain of NusG binds to Rho and strongly stimulates its activity in vivo and in vitro 67 Elucidation of the phosphorylation chain leading to inactivation of GlcT. Table antirermination Antitermination regulators in bacteria and phages. In the second mechanism, transfer RNA is used as the regulator.


Transcription attenuation.

In the case of the amino acid operons, insufficient levels of the amino acid leads to increased expression of the corresponding biosynthetic attenuatiln. Under inducing conditions extracellular tryptophanribosome stalling at the tnaC stop codon prevents Rho association, leading to transcription readthrough.

NusG is a component of the complete antitermination complex and enhances N antitermination in vitro. RfaH and the ops element, components of a novel system controlling bacterial transcription elongation.


The tryptophanase operon of Proteus vulgaris is thought to be regulated by a mechanism essentially identical to that of E. Views Read Edit View history. Passive, site-specific antiterminators encoded by phages. Gong F, Yanofsky C. When pN recognizes the nut site, it forms a persistent antitermination complex in cooperation with a number of E.

In one model, translating ribosomes occlude the nascent RNA, blocking the binding of Rho to the rut element. Aminoacylation of this tRNA is predicted to interfere with the interaction at the CCA end and prevent the charged tRNA from binding; the leader transcript then folds into the conformation with the terminator, halting transcription.