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...
Main Authors: | , , , , |
---|---|
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 |