Table of Contents    
ARTICLE
Year : 2011  |  Volume : 2  |  Issue : 3  |  Page : 129  

Tracing functional divergence and positive selection in NifH/Bchl protein family


1 NBU Bioinformatics Facility, Department of Botany, University of North Bengal, Siliguri 734013, India
2 Bioinformatics Chemoinformatics Laboratory, Department of Chemistry, Raiganj College, Raiganj, India

Date of Web Publication26-May-2012

Correspondence Address:
Subarna Thakur
NBU Bioinformatics Facility, Department of Botany, University of North Bengal, Siliguri 734013
India
Login to access the Email id

Source of Support: None, Conflict of Interest: None


Rights and PermissionsRights and Permissions

How to cite this article:
Thakur S, Bothra AK, Sen A. Tracing functional divergence and positive selection in NifH/Bchl protein family. J Nat Sc Biol Med 2011;2, Suppl S1:129

How to cite this URL:
Thakur S, Bothra AK, Sen A. Tracing functional divergence and positive selection in NifH/Bchl protein family. J Nat Sc Biol Med [serial online] 2011 [cited 2020 Feb 24];2, Suppl S1:129. Available from: http://www.jnsbm.org/text.asp?2011/2/3/129/96250

The ability to fix nitrogen is found in most major groups of bacteria and in some methanogenic archaea. The emergence and evolution of nitrogen fixation ability (diazotrophy) among Prokaryotes is complex and has not yet been fully elucidated. All N 2 -fixing organisms depend on nitrogenase for the conversion of atmospheric nitrogen to ammonia. The nitrogenase enzyme is a two-component system that consists of the iron protein (Fe-protein or NifH) and molybdenum-iron protein (MoFe-protein) working in tandem to effect nitrogen reduction. A number of proteins have structural and mechanistic similarities as well as evolutionary relationships with the NifH protein, notable among them being the light independent protochlorophyllidae reducatse (Bchl) which belong to the same superfamily of metalloproteins. In order to elucidate intrinsic functional diversity, and underlying evolutionary mechanism among NifH protein, we performed comprehensive bioinformatics analysis NifH/Bchl family. To estimate functional divergence in the NifH/Bchl family, we have conducted pair-wise functional divergence analysis between nifH paralogous genes using DIVERGE program. Our results show that NifH protein paralogs evolved from several gene duplication events followed by functional divergence. We identified a number of protein domains, and amino acid residues which contribute to predicted functional divergence. We have also made use of the maximum likelihood tests for detection of positive selection at the amino acid level. The structure based phylogenetic approach was also applied to draw conclusion on the ancient divergence and novel characterization of the NifH/Bchl protein family. The 3D structure based phylogenetic tree suggests that NifH protein and ChlL (FywA) share maximum similarities and have probably diverged most recently compared to others. It also suggests that both NifH and ChlL could have evolved from a MinD protein like ancestor.




 

Top
  
 
  Search
 
    Similar in PUBMED
   Search Pubmed for
   Search in Google Scholar for
    Access Statistics
    Email Alert *
    Add to My List *
* Registration required (free)  

 
  In this article

 Article Access Statistics
    Viewed881    
    Printed42    
    Emailed0    
    PDF Downloaded131    
    Comments [Add]    

Recommend this journal