Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.

ADP-glucose pyrophosphorylase (AGPase), a key allosteric enzyme involved in higher plant starch biosynthesis, is composed of pairs of large (LS) and small subunits (SS). Current evidence indicates that the two subunit types play distinct roles in enzyme function. Recently the heterotetrameric struct...

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Autores principales:	Ibrahim Baris, Aytug Tuncel, Natali Ozber, Ozlem Keskin, Ibrahim Halil Kavakli
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/87f10889a2c644ae977903691ed08af7
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spelling	oai:doaj.org-article:87f10889a2c644ae977903691ed08af72021-11-25T05:42:52ZInvestigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.1553-734X1553-735810.1371/journal.pcbi.1000546https://doaj.org/article/87f10889a2c644ae977903691ed08af72009-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19876371/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358ADP-glucose pyrophosphorylase (AGPase), a key allosteric enzyme involved in higher plant starch biosynthesis, is composed of pairs of large (LS) and small subunits (SS). Current evidence indicates that the two subunit types play distinct roles in enzyme function. Recently the heterotetrameric structure of potato AGPase has been modeled. In the current study, we have applied the molecular mechanics generalized born surface area (MM-GBSA) method and identified critical amino acids of the potato AGPase LS and SS subunits that interact with each other during the native heterotetrameric structure formation. We have further shown the role of the LS amino acids in subunit-subunit interaction by yeast two-hybrid, bacterial complementation assay and native gel. Comparison of the computational results with the experiments has indicated that the backbone energy contribution (rather than the side chain energies) of the interface residues is more important in identifying critical residues. We have found that lateral interaction of the LS-SS is much stronger than the longitudinal one, and it is mainly mediated by hydrophobic interactions. This study will not only enhance our understanding of the interaction between the SS and the LS of AGPase, but will also enable us to engineer proteins to obtain better assembled variants of AGPase which can be used for the improvement of plant yield.Ibrahim BarisAytug TuncelNatali OzberOzlem KeskinIbrahim Halil KavakliPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 5, Iss 10, p e1000546 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Ibrahim Baris Aytug Tuncel Natali Ozber Ozlem Keskin Ibrahim Halil Kavakli Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
description	ADP-glucose pyrophosphorylase (AGPase), a key allosteric enzyme involved in higher plant starch biosynthesis, is composed of pairs of large (LS) and small subunits (SS). Current evidence indicates that the two subunit types play distinct roles in enzyme function. Recently the heterotetrameric structure of potato AGPase has been modeled. In the current study, we have applied the molecular mechanics generalized born surface area (MM-GBSA) method and identified critical amino acids of the potato AGPase LS and SS subunits that interact with each other during the native heterotetrameric structure formation. We have further shown the role of the LS amino acids in subunit-subunit interaction by yeast two-hybrid, bacterial complementation assay and native gel. Comparison of the computational results with the experiments has indicated that the backbone energy contribution (rather than the side chain energies) of the interface residues is more important in identifying critical residues. We have found that lateral interaction of the LS-SS is much stronger than the longitudinal one, and it is mainly mediated by hydrophobic interactions. This study will not only enhance our understanding of the interaction between the SS and the LS of AGPase, but will also enable us to engineer proteins to obtain better assembled variants of AGPase which can be used for the improvement of plant yield.
format	article
author	Ibrahim Baris Aytug Tuncel Natali Ozber Ozlem Keskin Ibrahim Halil Kavakli
author_facet	Ibrahim Baris Aytug Tuncel Natali Ozber Ozlem Keskin Ibrahim Halil Kavakli
author_sort	Ibrahim Baris
title	Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
title_short	Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
title_full	Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
title_fullStr	Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
title_full_unstemmed	Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
title_sort	investigation of the interaction between the large and small subunits of potato adp-glucose pyrophosphorylase.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/87f10889a2c644ae977903691ed08af7
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Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.

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