scholarly journals Characterization of Chlamydomonas reinhardtiiZygote-Specific cDNAs That Encode Novel Proteins Containing Ankyrin Repeats and WW Domains

1999 ◽  
Vol 119 (3) ◽  
pp. 873-884 ◽  
Author(s):  
Hideo Kuriyama ◽  
Hiroyoshi Takano ◽  
Lena Suzuki ◽  
Hidenobu Uchida ◽  
Shigeyuki Kawano ◽  
...  
2004 ◽  
Vol 15 (5) ◽  
pp. 2287-2301 ◽  
Author(s):  
Srinivas Venkatram ◽  
Joseph J. Tasto ◽  
Anna Feoktistova ◽  
Jennifer L. Jennings ◽  
Andrew J. Link ◽  
...  

The γ-tubulin complex, via its ability to organize microtubules, is critical for accurate chromosome segregation and cytokinesis in the fission yeast, Schizosaccharomyces pombe. To better understand its roles, we have purified the S. pombe γ-tubulin complex. Mass spectrometric analyses of the purified complex revealed known components and identified two novel proteins (i.e., Mbo1p and Gfh1p) with homology to γ-tubulin–associated proteins from other organisms. We show that both Mbo1p and Gfh1p localize to microtubule organizing centers. Although cells deleted for either mbo1+ or gfh1+ are viable, they exhibit a number of defects associated with altered microtubule function such as defects in cell polarity, nuclear positioning, spindle orientation, and cleavage site specification. In addition, mbo1Δ and gfh1Δ cells exhibit defects in astral microtubule formation and anchoring, suggesting that these proteins have specific roles in astral microtubule function. This study expands the known roles of γ-tubulin complex components in organizing different types of microtubule structures in S. pombe.


FEBS Letters ◽  
2015 ◽  
Vol 589 (15) ◽  
pp. 1935-1942 ◽  
Author(s):  
Jiahong Jiang ◽  
Nan Wang ◽  
Yafei Jiang ◽  
Hongwei Tan ◽  
Jimin Zheng ◽  
...  
Keyword(s):  

Microbiology ◽  
2014 ◽  
Vol 160 (1) ◽  
pp. 149-164 ◽  
Author(s):  
Luis G. V. Fernandes ◽  
Monica L. Vieira ◽  
Ivy J. Alves ◽  
Zenaide M. de Morais ◽  
Silvio A. Vasconcellos ◽  
...  

This work shows the production and characterization of two novel putative lipoproteins encoded by the genes LIC10645 and LIC10731 identified in the genome sequences of Leptospira interrogans. In silico conservation analysis indicated that the proteins are well conserved among pathogenic leptospiral serovars and species. Recombinant proteins were obtained in Escherichia coli BL21(DE3) Star pLysS strain, purified by metal-affinity chromatography, and used for characterization and immunological evaluations. Recombinant proteins were capable of eliciting a combination of humoral and cellular immune responses in animal models, and could be recognized by antibodies present in human serum samples. The recombinant proteins Lsa44 and Lsa45 were able to bind laminin, and were named Lsa44 and Lsa45 for leptospiral surface adhesins of 44 and 45 kDa, respectively. The attachment to laminin was dose-responsive with K D values of 108.21 and 250.38 nM for Lsa44 and Lsa45, respectively. Moreover, these proteins interact with plasminogen (PLG) with K D values of 53.56 and 36.80 nM, respectively. PLG bound to the recombinant proteins could be converted to plasmin (PLA) in the presence of an activator. Cellular localization assays suggested that the Lsa44 and Lsa45 were surface-exposed. These are versatile proteins capable of interacting with laminin and PLG/PLA, and hence could mediate bacterial adhesion and contribute to tissue penetration.


Author(s):  
Sandhya Mishra ◽  
Ziqiu Lin ◽  
Shimei Pang ◽  
Wenping Zhang ◽  
Pankaj Bhatt ◽  
...  

Global environmental contamination with a complex mixture of xenobiotics has become a major environmental issue worldwide. Many xenobiotic compounds severely impact the environment due to their high toxicity, prolonged persistence, and limited biodegradability. Microbial-assisted degradation of xenobiotic compounds is considered to be the most effective and beneficial approach. Microorganisms have remarkable catabolic potential, with genes, enzymes, and degradation pathways implicated in the process of biodegradation. A number of microbes, including Alcaligenes, Cellulosimicrobium, Microbacterium, Micrococcus, Methanospirillum, Aeromonas, Sphingobium, Flavobacterium, Rhodococcus, Aspergillus, Penecillium, Trichoderma, Streptomyces, Rhodotorula, Candida, and Aureobasidium, have been isolated and characterized, and have shown exceptional biodegradation potential for a variety of xenobiotic contaminants from soil/water environments. Microorganisms potentially utilize xenobiotic contaminants as carbon or nitrogen sources to sustain their growth and metabolic activities. Diverse microbial populations survive in harsh contaminated environments, exhibiting a significant biodegradation potential to degrade and transform pollutants. However, the study of such microbial populations requires a more advanced and multifaceted approach. Currently, multiple advanced approaches, including metagenomics, proteomics, transcriptomics, and metabolomics, are successfully employed for the characterization of pollutant-degrading microorganisms, their metabolic machinery, novel proteins, and catabolic genes involved in the degradation process. These technologies are highly sophisticated, and efficient for obtaining information about the genetic diversity and community structures of microorganisms. Advanced molecular technologies used for the characterization of complex microbial communities give an in-depth understanding of their structural and functional aspects, and help to resolve issues related to the biodegradation potential of microorganisms. This review article discusses the biodegradation potential of microorganisms and provides insights into recent advances and omics approaches employed for the specific characterization of xenobiotic-degrading microorganisms from contaminated environments.


2000 ◽  
Vol 296 (4) ◽  
pp. 1139-1152 ◽  
Author(s):  
Walter A Koppensteiner ◽  
Peter Lackner ◽  
Markus Wiederstein ◽  
Manfred J Sippl

2003 ◽  
Vol 85 (3) ◽  
pp. 717-728 ◽  
Author(s):  
V. Pignot ◽  
A. E. Hein ◽  
C. Barske ◽  
C. Wiessner ◽  
A. R. Walmsley ◽  
...  
Keyword(s):  

2020 ◽  
Author(s):  
Simona Amodeo ◽  
Anneliese Hoffmann ◽  
Albert Fradera-Sola ◽  
Irina Bregy ◽  
Hélène Baudouin ◽  
...  

AbstractTrypanosoma brucei is a single celled eukaryotic parasite in the group of the Excavates. T. brucei cells harbor a single mitochondrion with a singular mitochondrial genome, that consists of a unique network of thousands of interwoven circular DNA molecule copies and is termed the kinetoplast DNA (kDNA). To ensure proper inheritance of the kDNA to the daughter cells the genome is linked to the basal body, the master organizer of the cell cycle in trypanosomes. The structure connecting the basal body and kDNA is termed the tripartite attachment complex (TAC). Using a combination of proteomics and RNAi (depletomics) we test the current model of hierarchical TAC assembly and identify TbmtHMG44 and Tb927.11.16120 as novel candidates of a structure that connects the TAC to the kDNA. Both proteins localize in the region of the unilateral filaments between TAC102 and the kDNA and depletion of each leads to a strong kDNA loss phenotype. TbmtHMG44 and Tb927.11.16120 stably associate with extracted flagella, even after DNase treatment however they do require the kDNA for initial assembly. Furthermore we demonstrate that recombinant Tb927.11.16120 is a DNA binding protein and thus a promising candidate to link the TAC to the kDNA.


Sign in / Sign up

Export Citation Format

Share Document