scholarly journals Nucleolar Structure and Function in Trypanosomatid Protozoa

Cells ◽  
2019 ◽  
Vol 8 (5) ◽  
pp. 421 ◽  
Author(s):  
Santiago Martínez-Calvillo ◽  
Luis E. Florencio-Martínez ◽  
Tomás Nepomuceno-Mejía

The nucleolus is the conspicuous nuclear body where ribosomal RNA genes are transcribed by RNA polymerase I, pre-ribosomal RNA is processed, and ribosomal subunits are assembled. Other important functions have been attributed to the nucleolus over the years. Here we review the current knowledge about the structure and function of the nucleolus in the trypanosomatid parasites Trypanosoma brucei, Trypanosoma cruzi and Leishmania ssp., which represent one of the earliest branching lineages among the eukaryotes. These protozoan parasites present a single nucleolus that is preserved throughout the closed nuclear division, and that seems to lack fibrillar centers. Trypanosomatids possess a relatively low number of rRNA genes, which encode rRNA molecules that contain large expansion segments, including several that are trypanosomatid-specific. Notably, the large subunit rRNA (28S-type) is fragmented into two large and four small rRNA species. Hence, compared to other organisms, the rRNA primary transcript requires additional processing steps in trypanosomatids. Accordingly, this group of parasites contains the highest number ever reported of snoRNAs that participate in rRNA processing. The number of modified rRNA nucleotides in trypanosomatids is also higher than in other organisms. Regarding the structure and biogenesis of the ribosomes, recent cryo-electron microscopy analyses have revealed several trypanosomatid-specific features that are discussed here. Additional functions of the nucleolus in trypanosomatids are also reviewed.

Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins

Correlations between structure and function of biological macromolecules have been studied intensively for many years, mostly by indirect methods. High resolution electron microscopy is a unique tool which can provide such information directly by comparing the conformation of biopolymers in their biologically active and inactive state. We have correlated the structure and function of ribosomes, ribonucleoprotein particles which are the site of protein biosynthesis. 70S E. coli ribosomes, used in this experiment, are composed of two subunits - large (50S) and small (30S). The large subunit consists of 34 proteins and two different ribonucleic acid molecules. The small subunit contains 21 proteins and one RNA molecule. All proteins (with the exception of L7 and L12) are present in one copy per ribosome.This study deals with the changes in the fine structure of E. coli ribosomes depleted of proteins L7 and L12. These proteins are unique in many aspects.


1999 ◽  
Vol 79 (1) ◽  
pp. S23-S45 ◽  
Author(s):  
DAVID N. SHEPPARD ◽  
MICHAEL J. WELSH

Sheppard, David N., and Michael J. Welsh. Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79 , Suppl.: S23–S45, 1999. — The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl− channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.


1985 ◽  
Vol 8 (3-4) ◽  
pp. 747-755 ◽  
Author(s):  
Harry F. Noller ◽  
Barbara J. Van Stolk ◽  
Danesh Moazed ◽  
Stephen Douthwaite ◽  
Robin R. Gutell

2019 ◽  
Vol 20 (6) ◽  
pp. 1353 ◽  
Author(s):  
Quan Wang ◽  
Sha Yang ◽  
Shubo Wan ◽  
Xinguo Li

As a secondary messenger, calcium participates in various physiological and biochemical reactions in plants. Photosynthesis is the most extensive biosynthesis process on Earth. To date, researchers have found that some chloroplast proteins have Ca2+-binding sites, and the structure and function of some of these proteins have been discussed in detail. Although the roles of Ca2+ signal transduction related to photosynthesis have been discussed, the relationship between calcium and photosynthesis is seldom systematically summarized. In this review, we provide an overview of current knowledge of calcium’s role in photosynthesis.


Parasitology ◽  
2004 ◽  
Vol 130 (2) ◽  
pp. 157-167 ◽  
Author(s):  
H. SATO ◽  
A. OSANAI ◽  
H. KAMIYA ◽  
Y. OBARA ◽  
W. JIANG ◽  
...  

Trypanosoma (Herpetosoma) grosi, which naturally parasitizesApodemusspp., can experimentally infect Mongolian jirds (Meriones unguiculatus). Three isolates fromA. agrarius,A. peninsulae, andA. speciosus(named SESUJI, HANTO, and AKHA isolates, respectively) of different geographical origin (AKHA from Japan, and the others from Vladivostok), exhibited different durations of parasitaemia in laboratory jirds (2 weeks for HANTO, and 3 weeks for the others). To assess the genetic background of theseT. grosiisolates, their small (SSU) and large subunit (LSU) ribosomal RNA genes (rDNA) were sequenced along with those of 2 otherHerpetosomaspecies from squirrels. The SSU rDNA sequences of these 3 species along with available sequences of 3 otherHerpetosomatrypanosomes (T. lewisi,T. musculiandT. microti)seemed to reflect well the phylogenetic relationship of their hosts. Three isolates ofT. grosiexhibited base changes at 2–6 positions of 2019-base 18S rDNA, at 5–29 positions of 1817/1818-base 28Sα rDNA, or 1–5 positions of 1557–1559-base 28Sβ rDNA, and none was separated from the other 2 isolates by rDNA nucleotide sequences. Since base changes ofHerpetosomatrypanosomes at the level of inter- and intra-species might occur frequently in specified rDNA regions, the molecular analysis on these regions of rodent trypanosomes could help species/strain differentiation and systematic revision ofHerpetosomatrypanosome species, which must be more abundant than presently known.


2019 ◽  
Vol 65 (3) ◽  
pp. 191-200 ◽  
Author(s):  
Yu Wang ◽  
Jinsheng Sun ◽  
Enjun Fang ◽  
Biao Guo ◽  
Yuanyuan Dai ◽  
...  

Artificial reefs have significantly altered ecological and environmental conditions compared with natural reefs, but how these changes affect sediment bacteria structure and function is unknown. Here, we compared the structure and function of the sediment bacterial community in the artificial reef area, the future artificial reef area, and the control area in Bohai Bay by 16S rRNA genes sequencing. Our results indicated that bacteria communities in the sediment were both taxonomically and functionally different between the reef area and control area. In the artificial reef area, the α-diversity was significantly lower, whereas the β-diversity was significantly higher. Functional genes related to chemo-heterotrophy, nitrate reduction, hydrocarbon degradation, and the human pathogens and human gut were more abundant, whereas genes related to the metabolism of sulfur compounds were less abundant in the artificial reef than in the control area. The differences in bacterial communities were primarily determined by depth in the artificial reef area, and by total organic carbon in the future reef area and control area. This study provides the first overview of molecular ecology to assess the impacts of artificial reefs on the bacteria community.


2020 ◽  
Vol 36 (11) ◽  
pp. 3365-3371
Author(s):  
Yaxin Xue ◽  
Anders Lanzén ◽  
Inge Jonassen

Abstract Motivation Technological advances in meta-transcriptomics have enabled a deeper understanding of the structure and function of microbial communities. ‘Total RNA’ meta-transcriptomics, sequencing of total reverse transcribed RNA, provides a unique opportunity to investigate both the structure and function of active microbial communities from all three domains of life simultaneously. A major step of this approach is the reconstruction of full-length taxonomic marker genes such as the small subunit ribosomal RNA. However, current tools for this purpose are mainly targeted towards analysis of amplicon and metagenomic data and thus lack the ability to handle the massive and complex datasets typically resulting from total RNA experiments. Results In this work, we introduce MetaRib, a new tool for reconstructing ribosomal gene sequences from total RNA meta-transcriptomic data. MetaRib is based on the popular rRNA assembly program EMIRGE, together with several improvements. We address the challenge posed by large complex datasets by integrating sub-assembly, dereplication and mapping in an iterative approach, with additional post-processing steps. We applied the method to both simulated and real-world datasets. Our results show that MetaRib can deal with larger datasets and recover more rRNA genes, which achieve around 60 times speedup and higher F1 score compared to EMIRGE in simulated datasets. In the real-world dataset, it shows similar trends but recovers more contigs compared with a previous analysis based on random sub-sampling, while enabling the comparison of individual contig abundances across samples for the first time. Availability and implementation The source code of MetaRib is freely available at https://github.com/yxxue/MetaRib. Contact [email protected] or [email protected] Supplementary information Supplementary data are available at Bioinformatics online.


Mathematics ◽  
2020 ◽  
Vol 8 (9) ◽  
pp. 1467
Author(s):  
Anastasia Mozokhina ◽  
Rostislav Savinkov

This paper presents current knowledge about the structure and function of the lymphatic system. Mathematical models of lymph flow in the single lymphangion, the series of lymphangions, the lymph nodes, and the whole lymphatic system are considered. The main results and further perspectives are discussed.


1981 ◽  
Vol 59 (4) ◽  
pp. 280-289 ◽  
Author(s):  
Norman P. A. Huner ◽  
Jiwan P. Palta ◽  
Paul H. Li ◽  
John V. Carter

A comparison of ribulosebisphosphate carboxylase–oxygenase from the leaves of the non-acclimated, cold-hardy species, Solanum commersonii, and the nonacclimated, nonhardy species, Solanum tuberosum showed that this enzyme from the two species differed in structure and function. The results of sulfhydryl group titration with 5,5′-dithiobis(2-nitrobenzoic acid) indicated that the kinetics of titration and the number of accessible sulfhydryl groups in the native enzymes were different. After 30 min, the enzyme from the hardy species had 1.7 times fewer sulfhydryl groups titrated than that from the nonhardy species. In the presence of 1% (w/v) sodium dodecyl sulfate, the total number of sulfhydryl groups titratable with 5,5′-dithiobis-(2-nitrobenzoic acid) was the same for both species. However, this denaturant had a differential effect on the kinetics of titration with 5,5′-dithiobis(2-nitrobenzoic acid). Both enzymes had a native molecular weight of about 550 000. The quaternary structures of the two enzymes were similar with the presence of large and small subunits of 54 000 and 14 000, respectively. However, there was more polypeptide of 108 000 – 110 000 present in preparations of the enzyme from S. tuberosum than from S. commersonii. This polypeptide is an apparent dimer of the large subunit on a relative mass basis. The large subunit of the enzyme from S. tuberosum was more sensitive to the absence of reducing agent and was more sensitive to freezing and thawing than the large subunit of the enzyme from S. commersonii. Catalytic properties of both enzymes at 5 and 25 °C indicated no significant difference in the [Formula: see text] at either temperature. However, the Vmax at 5 °C for the enzyme from S. commersonii was 35% higher than that of the enzyme from S. tuberosum. In contrast, the Vmax at 25 °C for the enzyme of the hardy species was 250% lower than that of the enzyme from the nonhardy species.


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