Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.

H(+)-translocating inorganic pyrophosphatases (H(+)-PPase) were recognized as the original energy donors in the development of plants. A large number of researchers have shown that H(+)-PPase could be an early-originated protein that participated in many important biochemical and physiological proce...

Full description

Bibliographic Details
Main Authors: Yanqin Wang, Shuangxia Jin, Maojun Wang, Longfu Zhu, Xianlong Zhang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3726567?pdf=render
id doaj-5afbdc4fad674ebeabe0eea6416be157
record_format Article
spelling doaj-5afbdc4fad674ebeabe0eea6416be1572020-11-24T21:50:26ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0187e7009910.1371/journal.pone.0070099Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.Yanqin WangShuangxia JinMaojun WangLongfu ZhuXianlong ZhangH(+)-translocating inorganic pyrophosphatases (H(+)-PPase) were recognized as the original energy donors in the development of plants. A large number of researchers have shown that H(+)-PPase could be an early-originated protein that participated in many important biochemical and physiological processes. In this study we cloned 14 novel sequences from 7 eremophytes: Sophora alopecuroid (Sa), Glycyrrhiza uralensis (Gu), Glycyrrhiza inflata (Gi), Suaeda salsa (Ss), Suaeda rigida (Sr), Halostachys caspica (Hc), and Karelinia caspia (Kc). These novel sequences included 6 ORFs and 8 fragments, and they were identified as H(+)-PPases based on the typical conserved domains. Besides the identified domains, sequence alignment showed that there still were two novel conserved motifs. A phylogenetic tree was constructed, including the 14 novel H(+)-PPase amino acid sequences and the other 34 identified H(+)-PPase protein sequences representing plants, algae, protozoans and bacteria. It was shown that these 48 H(+)-PPases were classified into two groups: type I and type II H(+)-PPase. The novel 14 eremophyte H(+)-PPases were classified into the type I H(+)-PPase. The 3D structures of these H(+)-PPase proteins were predicted, which suggested that all type I H(+)-PPases from higher plants and algae were homodimers, while other type I H(+)-PPases from bacteria and protozoans and all type II H(+)-PPases were monomers. The 3D structures of these novel H(+)-PPases were homodimers except for SaVP3, which was a monomer. This regular structure could provide important evidence for the evolutionary origin and study of the relationship between the structure and function among members of the H(+)-PPase family.http://europepmc.org/articles/PMC3726567?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Yanqin Wang
Shuangxia Jin
Maojun Wang
Longfu Zhu
Xianlong Zhang
spellingShingle Yanqin Wang
Shuangxia Jin
Maojun Wang
Longfu Zhu
Xianlong Zhang
Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.
PLoS ONE
author_facet Yanqin Wang
Shuangxia Jin
Maojun Wang
Longfu Zhu
Xianlong Zhang
author_sort Yanqin Wang
title Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.
title_short Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.
title_full Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.
title_fullStr Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.
title_full_unstemmed Isolation and characterization of a conserved domain in the eremophyte H+-PPase family.
title_sort isolation and characterization of a conserved domain in the eremophyte h+-ppase family.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2013-01-01
description H(+)-translocating inorganic pyrophosphatases (H(+)-PPase) were recognized as the original energy donors in the development of plants. A large number of researchers have shown that H(+)-PPase could be an early-originated protein that participated in many important biochemical and physiological processes. In this study we cloned 14 novel sequences from 7 eremophytes: Sophora alopecuroid (Sa), Glycyrrhiza uralensis (Gu), Glycyrrhiza inflata (Gi), Suaeda salsa (Ss), Suaeda rigida (Sr), Halostachys caspica (Hc), and Karelinia caspia (Kc). These novel sequences included 6 ORFs and 8 fragments, and they were identified as H(+)-PPases based on the typical conserved domains. Besides the identified domains, sequence alignment showed that there still were two novel conserved motifs. A phylogenetic tree was constructed, including the 14 novel H(+)-PPase amino acid sequences and the other 34 identified H(+)-PPase protein sequences representing plants, algae, protozoans and bacteria. It was shown that these 48 H(+)-PPases were classified into two groups: type I and type II H(+)-PPase. The novel 14 eremophyte H(+)-PPases were classified into the type I H(+)-PPase. The 3D structures of these H(+)-PPase proteins were predicted, which suggested that all type I H(+)-PPases from higher plants and algae were homodimers, while other type I H(+)-PPases from bacteria and protozoans and all type II H(+)-PPases were monomers. The 3D structures of these novel H(+)-PPases were homodimers except for SaVP3, which was a monomer. This regular structure could provide important evidence for the evolutionary origin and study of the relationship between the structure and function among members of the H(+)-PPase family.
url http://europepmc.org/articles/PMC3726567?pdf=render
work_keys_str_mv AT yanqinwang isolationandcharacterizationofaconserveddomainintheeremophytehppasefamily
AT shuangxiajin isolationandcharacterizationofaconserveddomainintheeremophytehppasefamily
AT maojunwang isolationandcharacterizationofaconserveddomainintheeremophytehppasefamily
AT longfuzhu isolationandcharacterizationofaconserveddomainintheeremophytehppasefamily
AT xianlongzhang isolationandcharacterizationofaconserveddomainintheeremophytehppasefamily
_version_ 1725883986588205056