Accumulation of Species-Specific Amino Acid Replacements That Cause Loss of Particular Protein Functions in Buchnera, an Endocellular Bacterial Symbiont

2001 ◽  
Vol 53 (4-5) ◽  
pp. 377-386 ◽  
Author(s):  
Shuji Shigenobu ◽  
Hidemi Watanabe ◽  
Yoshiyuki Sakaki ◽  
Hajime Ishikawa
2009 ◽  
Vol 91 (2) ◽  
pp. 101-109 ◽  
Author(s):  
LI WANG ◽  
GANG LI ◽  
JINHONG WANG ◽  
SHAOHUI YE ◽  
GARETH JONES ◽  
...  

SummaryGap junction protein connexin43 (Cx43), encoded by the GJA1 gene, is the most abundant connexin in the cardiovascular system and was reported as a crucial factor maintaining cardiac electrical conduction, as well as having a very important function in facilitating the recycling of potassium ions from hair cells in the cochlea back into the cochlear endolymph during auditory transduction processes. In mammals, bats are the only taxon possessing powered flight, placing exceptional demand on many organismal processes. To meet the demands of flying, the hearts of bats show many specialties. Moreover, ultrasonic echolocation allows bat species to orientate and often detect and locate food in darkness. In this study, we cloned the full-length coding region of GJA1 gene from 12 different species of bats and obtained orthologous sequences from other mammals. We used the maximum likelihood method to analyse the evolution of GJA1 gene in mammals and the lineage of bats. Our results showed this gene is much conserved in mammals, as well as in bats' lineage. Compared with other mammals, we found one private amino acid substitution shared by bats, which is located on the inner loop domain, as well as some species-specific amino acid substitutions. The evolution rate analyses showed the signature of purifying selection on not only different classification level lineages but also the different domains and amino acid residue sites of this gene. Also, we suggested that GJA1 gene could be used as a good molecular marker to do the phylogenetic reconstruction.


2010 ◽  
Vol 55 (1) ◽  
pp. 368-372 ◽  
Author(s):  
María-José Ferrándiz ◽  
Carmen Ardanuy ◽  
Josefina Liñares ◽  
Luz Balsalobre ◽  
María Teresa García ◽  
...  

ABSTRACTEight rifampin-resistant streptococci of the mitis group were identified at the species level by using a concatenated 16S rRNA gene-sodA-rpoB-hlpAsequence. Characterization of theirrpoBalleles showed single amino acid changes involved in rifampin resistance. Comparison of RpoB sequences from pneumococcal recombinant isolates, viridans isolates, and type strains revealed a species-specific amino acid signature, which allowed it to be ascertained that recombinant RpoBs were originated in genetic interchanges withStreptococcus mitisandStreptococcus oralis.


2018 ◽  
Vol 62 (8) ◽  
Author(s):  
Anne Bernhardt ◽  
Wieland Meyer ◽  
Volker Rickerts ◽  
Toni Aebischer ◽  
Kathrin Tintelnot

ABSTRACT Scedosporium spp. cause infections (scedosporiosis) in both immunocompetent and immunocompromised individuals and may persistently colonize the respiratory tract in patients with cystic fibrosis (CF). They are less susceptible against azoles than are other molds, such as Aspergillus spp., suggesting the presence of resistance mechanisms. It can be hypothesized that the decreased susceptibility of Scedosporium spp. to azoles is also CYP51 dependent. Analysis of the Scedosporium apiospermum and Scedosporium aurantiacum genomes revealed one CYP51 gene encoding the 14-α-lanosterol demethylase. This gene from 159 clinical or environmental Scedosporium isolates and three Lomentospora prolificans isolates has been sequenced and analyzed. The Scedosporium CYP51 protein clustered with the group of known CYP51B orthologues and showed species-specific polymorphisms. A tandem repeat in the 5′ upstream region of Scedosporium CYP51 like that in Aspergillus fumigatus could not be detected. Species-specific amino acid alterations in CYP51 of Scedosporium boydii, Scedosporium ellipsoideum, Scedosporium dehoogii, and Scedosporium minutisporum isolates were located at positions that have not been described as having an impact on azole susceptibility. In contrast, two of the three S. apiospermum-specific amino acid changes (Y136F and G464S) corresponded to respective mutations in A. fumigatus CYP51A at amino acid positions 121 and 448 (Y121F and G448S, respectively) that had been linked to azole resistance.


1975 ◽  
Vol 12 (6-7) ◽  
pp. 505-509 ◽  
Author(s):  
An-Chuan Wang ◽  
H. Hugh Fudenberg ◽  
Herve Bazin

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