Genome-wide characterization of Major Intrinsic Proteins (MIPs) family in Momordica charantia

Shifa Begum Shifa Begum,Ruhul A Khan Ruhul A Khan

doi:10.30574/gscbps.2022.18.2.0047

Shifa Begum Shifa Begum, Ruhul A Khan Ruhul A Khan

Open Access

https://doi.org/10.30574/gscbps.2022.18.2.0047

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Abstract

Major intrinsic proteins (MIPs) family include the group of proteins also called channel proteins or water channels. Aquaporins facilitate the transport of water and other uncharged small molecules, forming pores in cellular boundaries which help in plant growth, development, and sometimes in plant adaptation. They usually have six tranSmembrane alpha-helical domains with conserved amino acids residues along with hydrophobic and hydrophilic regions. Though aquaporins were found both in animals and plants, also in bacteria, fungi cells, it comprises the largest and most complex group in plant species. A little is known about the aquaporins family of the plant Momordica charantia. About 25 aquaporins of its are characterized in this study. The aquaporins of M. charantia are divided into five sub-families here, they are PIPs, TIPs, XIPs, SIPs, and NIPs. There are twelve PIPs, three TIPs, eight NIPs, and one AQPs in both XIP and SIP. In the XIP subfamily, it contains SPI other than the NPA motif. Moreover, SIP and NIP subfamily also contain different motifs both in loop B and loop E other than NPA motifs. McSIPs contain NPT in loop B and McNIPs contain NPS in loop B (McNIP1; 1, McNIP1; 3 and McNIP3; 1). Again, McNIPs contain NPV in loop E (McNIP2; 2, McNIP3; 1). The conserved residues and motifs of this plant show its transportation of water and the possibility of other molecules' transportation through those channel proteins.

Highlights

Aquaporins are small proteins (~30kDa) that locate in intracellular membranes or cytoplasmic membranes, function as channel proteins in the different types of cells as they form pores
Sequences encoding in the family Major intrinsic proteins (MIPs) include two NPA motifs with an amphipathic channel which indicates both the region of hydrophilic and hydrophobic were primarily selected as aquaporin
To exclude McNIP3; 2, it was further searched for predicted transmembrane domain in TMHMM and SOSUI (SOSUI result is not included in the result section, Appendix- Table 2), it showed four TMD both in TMHMM and SOSUI result

Summary

Introduction

Aquaporins are small proteins (~30kDa) that locate in intracellular membranes or cytoplasmic membranes, function as channel proteins in the different types of cells as they form pores These channel proteins help to transport fluids like water and other small polar molecules [1]. These are homologous water-channel proteins, found in both plants and animals They are water selective and/or pass small neutral solutes (urea, boric acid, silicic acid) or gases (ammonia, carbon dioxide) in the plant cells but ions or other metabolites cannot pass through the channels [2]. These channel proteins are providing an important role in plant and animal cells to facilitate and regulate the passage of water through their membranes [3]. Two short hydrophobic alpha-helices are on the opposite sides in the loops B and E, they are highly conserved NPA (Asn- Pro-Ala) motifs [5]

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