Bioinformatic analysis of the TonB protein family

BioMetals ◽  
2007 ◽  
Vol 20 (3-4) ◽  
pp. 467-483 ◽  
Author(s):  
Byron C. H. Chu ◽  
R. Sean Peacock ◽  
Hans J. Vogel
Mycologia ◽  
2013 ◽  
Vol 105 (6) ◽  
pp. 1479-1488 ◽  
Author(s):  
Hongxin Chen ◽  
Andriy Kovalchuk ◽  
Susanna Keriö ◽  
Fred O. Asiegbu

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Yacidzohara Rodríguez ◽  
Ricardo Gonzalez‐Mendez ◽  
Carmen Cadilla

2008 ◽  
Vol 72 (1) ◽  
pp. 13-53 ◽  
Author(s):  
Carol A. Bonner ◽  
Terrence Disz ◽  
Kaitlyn Hwang ◽  
Jian Song ◽  
Veronika Vonstein ◽  
...  

SUMMARY Many enzymes and other proteins are difficult subjects for bioinformatic analysis because they exhibit variant catalytic, structural, regulatory, and fusion mode features within a protein family whose sequences are not highly conserved. However, such features reflect dynamic and interesting scenarios of evolutionary importance. The value of experimental data obtained from individual organisms is instantly magnified to the extent that given features of the experimental organism can be projected upon related organisms. But how can one decide how far along the similarity scale it is reasonable to go before such inferences become doubtful? How can a credible picture of evolutionary events be deduced within the vertical trace of inheritance in combination with intervening events of lateral gene transfer (LGT)? We present a comprehensive analysis of a dehydrogenase protein family (TyrA) as a prototype example of how these goals can be accomplished through the use of cohesion group analysis. With this approach, the full collection of homologs is sorted into groups by a method that eliminates bias caused by an uneven representation of sequences from organisms whose phylogenetic spacing is not optimal. Each sufficiently populated cohesion group is phylogenetically coherent and defined by an overall congruence with a distinct section of the 16S rRNA gene tree. Exceptions that occasionally are found implicate a clearly defined LGT scenario whereby the recipient lineage is apparent and the donor lineage of the gene transferred is localized to those organisms that define the cohesion group. Systematic procedures to manage and organize otherwise overwhelming amounts of data are demonstrated.


2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.


2008 ◽  
Vol 35 (S 01) ◽  
Author(s):  
C Steinmetz ◽  
B von Einem ◽  
D Schwanzar ◽  
F Dolp ◽  
A.C Ludolph ◽  
...  

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