NDLI: A phylogenetic approach to study the origin and evolution of plasmodesmata-localized glycosyl hydrolases family 17

Content Provider	PubMed Central
Author	Rocio, Gaudioso-pedraza Benitez-alfonso, Yoselin
Copyright Year	2014
Abstract	Colonization of the land by plants required major modifications in cellular structural composition and metabolism. Intercellular communication through plasmodesmata (PD) plays a critical role in the coordination of growth and cell activities. Changes in the form, regulation or function of these channels are likely linked to plant adaptation to the terrestrial environments. Constriction of PD aperture by deposition of callose is the best-studied mechanism in PD regulation. Glycosyl hydrolases family 17 (GHL17) are callose degrading enzymes. In Arabidopsis this is a large protein family, few of which have been PD-localized. The objective here is to identify correlations between evolution of this protein family and their role at PD and to use this information as a tool to predict the localization of candidates isolated in a proteomic screen. With this aim, we studied phylogenetic relationship between Arabidopsis GHL17 sequences and those isolated from fungi, green algae, mosses and monocot representatives. Three distinct phylogenetic clades were identified. Clade alpha contained only embryophytes sequences suggesting that this subgroup appeared during land colonization in organisms with functional PD. Accordingly, all PD-associated GHL17 proteins identified so far in Arabidopsis thaliana and Populus are grouped in this ‘embryophytes only’ phylogenetic clade. Next, we tested the use of this knowledge to discriminate between candidates isolated in the PD proteome. Transient and stable expression of GFP protein fusions confirmed PD localization for candidates contained in clade alpha but not for candidates contained in clade beta. Our results suggest that GHL17 membrane proteins contained in the alpha clade evolved and expanded during land colonization to play new roles, among others, in PD regulation.
Related Links	http://dx.doi.org/10.3389/fpls.2014.00212
Starting Page	212
File Format	PDF
ISSN	1664462X
e-ISSN	1664462X
Journal	Frontiers in Plant Science
Volume Number	5
Language	English
Publisher	Frontiers Media S.A.
Publisher Date	2014-05-23
Access Restriction	Open
Rights Holder	Frontiers Media S.A.
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Plant Science

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

A phylogenetic approach to study the origin and evolution of the CRINKLY4 family

A phylogenetic approach to study the origin and evolution of the CRINKLY4 family

Evolution of Mammalian Chitinase(-Like) Members of Family 18 Glycosyl Hydrolases

Phylogenetic analyses suggest multiple changes of substrate specificity within the Glycosyl hydrolase 20 family

A Plasmodesmata-Localized Protein Mediates Crosstalk between Cell-to-Cell Communication and Innate Immunity in Arabidopsis [C] [W] [OA]

A Novel β-N-Acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: Gene Cloning, Expression, and Assignment to Family 3 of the Glycosyl Hydrolases

A phylogenetic approach to gene expression data: evidence for the evolutionary origin of mammalian leukocyte phenotypes

The DAG family of glycosyl hydrolases combines two previously identified protein families.

Determination of the Catalytic Base in Family 48 Glycosyl Hydrolases ▿

A phylogenetic approach to study the origin and evolution of plasmodesmata-localized glycosyl hydrolases family 17

Similar Documents

A phylogenetic approach to study the origin and evolution of the CRINKLY4 family

A phylogenetic approach to study the origin and evolution of the CRINKLY4 family

Evolution of Mammalian Chitinase(-Like) Members of Family 18 Glycosyl Hydrolases

Phylogenetic analyses suggest multiple changes of substrate specificity within the Glycosyl hydrolase 20 family

A Plasmodesmata-Localized Protein Mediates Crosstalk between Cell-to-Cell Communication and Innate Immunity in Arabidopsis [C] [W] [OA]

A Novel β-N-Acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: Gene Cloning, Expression, and Assignment to Family 3 of the Glycosyl Hydrolases

A phylogenetic approach to gene expression data: evidence for the evolutionary origin of mammalian leukocyte phenotypes

The DAG family of glycosyl hydrolases combines two previously identified protein families.

Determination of the Catalytic Base in Family 48 Glycosyl Hydrolases ▿

A phylogenetic approach to study the origin and evolution of plasmodesmata-localized glycosyl hydrolases family 17