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L7615 --> 486.5 --> In E. coli, transcription and translation are coupled and ribosomes can directly contact RNA polymerase. The contacts are formed between the RNA exit site of the RNA polymerase and ribosomal proteins uS2, uS3, or uS4 on the ribosome. We assessed the effects of ribosomal proteins uS2, uS3, and uS4 on transcription. In varying degrees, they all reduced termination and increased pausing. Although uS2 bound directly to the polymerase, it affected transcription the least. uS3, which did not bind the polymerase, had the most prominent effects on transcription. We suggest uS2 acts as an anchor for the polymerase during coupling of transcription and translation. Likewise, uS3 and uS4 may affect transcription depending on the length of RNA between the ribosome and polymerase. We speculate that ribosomal proteins may also coordinate the transcription of ribosomal RNAs with their assembly into ribosomes. Finally, we submit that the intrinsic effects of ribosomal proteins may drive the tight regulation of their expression in the cell. [ABSTRACT FROM AUTHOR]

Explores the concept of incest taboo in human beings. Instinctual female incest inhibition; Cultural father incest prohibition; Individual ontology of taboos; Plural nature of the incest taboo.

The coupling of transcription and translation is more than mere translation of an mRNA that is still being transcribed. The discovery of physical interactions between RNA polymerase and ribosomes has spurred renewed interest into this long-standing paradigm of bacterial molecular biology. Here, we provide a concise presentation of recent insights gained from super-resolution microscopy, biochemical, and structural work, including cryo-EM studies. Based on the presented data, we put forward a dynamic model for the interaction between RNA polymerase and ribosomes, in which the interactions are repeatedly formed and broken. Furthermore, we propose that long intervening nascent RNA will loop out and away during the forming the interactions between the RNA polymerase and ribosomes. By comparing the effect of the direct interactions between RNA polymerase and ribosomes with those that transcription factors NusG and RfaH mediate, we submit that two distinct modes of coupling exist: Factor-free and factor-mediated coupling. Finally, we provide a possible framework for transcription-translation coupling and elude to some open questions in the field. [ABSTRACT FROM AUTHOR]

The years since 2000 have been a golden age in in situ ocean observing with the proliferation and organization of autonomous platforms such as surface drogued buoys and subsurface Argo profiling floats augmenting ship-based observations. Global time series of mean sea surface temperature and ocean heat content are routinely calculated based on data from these platforms, enhancing our understanding of the ocean's role in Earth's climate system. Individual measurements of meteorological, sea surface, and subsurface variables directly improve our understanding of the Earth system, weather forecasting, and climate projections. They also provide the data necessary for validating and calibrating satellite observations. Maintaining this ocean observing system has been a technological, logistical, and funding challenge. The global COVID-19 pandemic, which took hold in 2020, added strain to the maintenance of the observing system. A survey of the contributing components of the observing system illustrates the impacts of the pandemic from January 2020 through December 2021. The pandemic did not reduce the short-term geographic coverage (days to months) capabilities mainly due to the continuation of autonomous platform observations. In contrast, the pandemic caused critical loss to longer-term (years to decades) observations, greatly impairing the monitoring of such crucial variables as ocean carbon and the state of the deep ocean. So, while the observing system has held under the stress of the pandemic, work must be done to restore the interrupted replenishment of the autonomous components and plan for more resilient methods to support components of the system that rely on cruise-based measurements. [ABSTRACT FROM AUTHOR]

The translational GTPase BipA regulates the expression of virulence and pathogenicity factors in several eubacteria. BipAdependent expression of virulence factors occurs under starvation conditions, such as encountered during infection of a host. Under these conditions, BipA associates with the small ribosomal subunit. BipA also has a second function to promote the efficiency of late steps in biogenesis of large ribosomal subunits at low temperatures, presumably while bound to the ribosome. During starvation, the cellular concentration of stress alarmone guanosine-3', 5'-bis pyrophosphate (ppGpp) is increased. This increase allows ppGpp to bind to BipA and switch its binding specificity from ribosomes to small ribosomal subunits. A conformational change of BipA upon ppGpp binding could explain the ppGpp regulation of the binding specificity of BipA. Here, we present the structures of the full-length BipA from Escherichia coli in apo, GDP-, and ppGpp-bound forms. The crystal structure and small-angle x-ray scattering data of the protein with bound nucleotides, together with a thermodynamic analysis of the binding of GDP and of ppGpp to BipA, indicate that the ppGpp-bound form of BipA adopts the structure of the GDP form. This suggests furthermore, that the switch in binding preference only occurs when both ppGpp and the small ribosomal subunit are present. This molecular mechanism would allow BipA to interact with both the ribosome and the small ribosomal subunit during stress response. [ABSTRACT FROM AUTHOR]

Summary: The Crp/Fnr family of transcriptional regulators play central roles in transcriptional control of diverse physiological responses, and are activated by a surprising diversity of mechanisms. MrpC is a Crp/Fnr homolog that controls the Myxococcus xanthus developmental program. A long‐standing model proposed that MrpC activity is controlled by the Pkn8/Pkn14 serine/threonine kinase cascade, which phosphorylates MrpC on threonine residue(s) located in its extreme amino‐terminus. In this study, we demonstrate that a stretch of consecutive threonine and serine residues, T21 T22 S23 S24, is necessary for MrpC activity by promoting efficient DNA binding. Mass spectrometry analysis indicated the TTSS motif is not directly phosphorylated by Pkn14 in vitro but is necessary for efficient Pkn14‐dependent phosphorylation on several residues in the remainder of the protein. In an important correction to a long‐standing model, we show Pkn8 and Pkn14 kinase activities do not play obvious roles in controlling MrpC activity in wild‐type M. xanthus under laboratory conditions. Instead, we propose Pkn14 modulates MrpC DNA binding in response to unknown environmental conditions. Interestingly, substitutions in the TTSS motif caused developmental defects that varied between biological replicates, revealing that MrpC plays a role in promoting a robust developmental phenotype. [ABSTRACT FROM AUTHOR]