A Novel Reversibly Glycosylated Polypeptide-2 of Bee Pollen from Rape (
MALDI-TOF-MS
Reversibly glycosylated polypeptide
Transmission Electron Microscope
immunological histological chemistry
peptide mass fingerprinting
rape bee pollen
Journal
Protein and peptide letters
ISSN: 1875-5305
Titre abrégé: Protein Pept Lett
Pays: Netherlands
ID NLM: 9441434
Informations de publication
Date de publication:
2021
2021
Historique:
received:
15
05
2020
revised:
15
09
2020
accepted:
15
09
2020
pubmed:
5
11
2020
medline:
2
7
2021
entrez:
4
11
2020
Statut:
ppublish
Résumé
Reversibly glycosylated polypeptide (RGP), a kind of hydrosoluble and plasmodesmal-associated protein found in plants, plays a crucial role in the development of pollen. A novel RGP 2 was isolated and identified from rape (Brassica napus L.) bee pollen. RGP2 was isolated and purified by ion-exchange column and gel filtration chromatography, and characterized by MALDI-TOF-MS, LC-MS, immunological histological chemistry, and transmission electron microscope. Our results indicated that the RGP2 is an acidic protein (pI=5.46) with the molecular weight 42388 Da. It contained 17 kinds of amino acids, among which aspartic acid had the highest amount (71.56 mg/g). Homologous alignment of amino acid sequence results showed that RGP2 was 80.33%, 85.02%, 86.06%, and 88.93% identical to Arabidopsis thaliana RGP2 (AtRGP2), Oryza sativa RGP (OsRGP), Triticum aestivum RGP (TaRGP), and Zea maize RGP (ZmRGP), respectively. The localization results showed that RGP2 in rape anther existed in exine and intine of anther cells of rape flower by immunological histological chemistry and the subcellular localization identified that RGP2 appeared around the Golgi apparatus in cytoplasm by transmission electron microscope. RGP2 has a highly conserved sequence of amino acid residues and potential glycosylation sites.
Sections du résumé
BACKGROUND
BACKGROUND
Reversibly glycosylated polypeptide (RGP), a kind of hydrosoluble and plasmodesmal-associated protein found in plants, plays a crucial role in the development of pollen.
OBJECTIVE
OBJECTIVE
A novel RGP 2 was isolated and identified from rape (Brassica napus L.) bee pollen.
METHODS
METHODS
RGP2 was isolated and purified by ion-exchange column and gel filtration chromatography, and characterized by MALDI-TOF-MS, LC-MS, immunological histological chemistry, and transmission electron microscope.
RESULTS
RESULTS
Our results indicated that the RGP2 is an acidic protein (pI=5.46) with the molecular weight 42388 Da. It contained 17 kinds of amino acids, among which aspartic acid had the highest amount (71.56 mg/g). Homologous alignment of amino acid sequence results showed that RGP2 was 80.33%, 85.02%, 86.06%, and 88.93% identical to Arabidopsis thaliana RGP2 (AtRGP2), Oryza sativa RGP (OsRGP), Triticum aestivum RGP (TaRGP), and Zea maize RGP (ZmRGP), respectively. The localization results showed that RGP2 in rape anther existed in exine and intine of anther cells of rape flower by immunological histological chemistry and the subcellular localization identified that RGP2 appeared around the Golgi apparatus in cytoplasm by transmission electron microscope.
CONCLUSION
CONCLUSIONS
RGP2 has a highly conserved sequence of amino acid residues and potential glycosylation sites.
Identifiants
pubmed: 33143610
pii: PPL-EPUB-111152
doi: 10.2174/0929866527666201103161302
doi:
Substances chimiques
Plant Proteins
0
Glucosyltransferases
EC 2.4.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
543-553Subventions
Organisme : National Natural Science Foundation of China
ID : 21978229, 21676212
Organisme : Key Research and Development Program of Shaanxi
ID : 2019NY-140
Organisme : Shaanxi Postdoctoral Science Foundation
ID : 2017BSHTDZZ14
Informations de copyright
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