» Articles » PMID: 8685275

Identification of a New Pea Gene, PsNlec1, Encoding a Lectin-like Glycoprotein Isolated from the Symbiosomes of Root Nodules

Overview
Journal Plant Physiol
Specialty Physiology
Date 1996 May 1
PMID 8685275
Citations 9
Authors
Affiliations
Soon will be listed here.
Abstract

A 27-kD glycoprotein antigen recognized by monoclonal antibody MAC266 was purified from isolated symbiosomes derived from pea (Pisum sativum) root nodules containing Rhizobium. The N-terminal amino acid sequence was obtained, and the corresponding cDNA clone was isolated by a polymerase chain reaction-based strategy. The clone contained a single open reading frame, and the gene was termed PsNlec1. Phylogenetic analysis of 31 legume sequences showed that the PsNlec1 protein is related to the legume lectin family but belongs to a subgroup that is very different from pea seed lectin. Expression of the PsNlec1 transcript was much stronger in nodules than in other parts of the plant. It was found in both infected and uninfected cells in the central tissue of the nodule and in the stele of the root near the attachment point of the nodule. When uninfected pea seedlings were grown on medium containing nitrate, weak transcription of PsNlec1 was observed in the root system. The identification of PsNlec1 inside the symbiosome is consistent with the observation that legume lectins are generally vacuolar proteins that may serve as transient storage components.

Citing Articles

Comparative analysis of remodelling of the plant-microbe interface in Pisum sativum and Medicago truncatula symbiotic nodules.

Tsyganova A, Seliverstova E, Brewin N, Tsyganov V Protoplasma. 2019; 256(4):983-996.

PMID: 30793221 DOI: 10.1007/s00709-019-01355-5.


The role of the cell wall compartment in mutualistic symbioses of plants.

Rich M, Schorderet M, Reinhardt D Front Plant Sci. 2014; 5:238.

PMID: 24917869 PMC: 4041022. DOI: 10.3389/fpls.2014.00238.


Differentiation of symbiotic cells and endosymbionts in Medicago truncatula nodulation are coupled to two transcriptome-switches.

Maunoury N, Redondo-Nieto M, Bourcy M, Van de Velde W, Alunni B, Laporte P PLoS One. 2010; 5(3):e9519.

PMID: 20209049 PMC: 2832008. DOI: 10.1371/journal.pone.0009519.


Plant lectins: the ties that bind in root symbiosis and plant defense.

Hoff P, Brill L, Hirsch A Mol Genet Genomics. 2009; 282(1):1-15.

PMID: 19488786 PMC: 2695554. DOI: 10.1007/s00438-009-0460-8.


Plant and bacterial symbiotic mutants define three transcriptionally distinct stages in the development of the Medicago truncatula/Sinorhizobium meliloti symbiosis.

Mitra R, Long S Plant Physiol. 2004; 134(2):595-604.

PMID: 14739349 PMC: 344536. DOI: 10.1104/pp.103.031518.


References
1.
Lund O, Engelbrecht J, Bohr H, Nielsen J, Hansen J . Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Biochem J. 1995; 308 ( Pt 3):801-13. PMC: 1136796. DOI: 10.1042/bj3080801. View

2.
Vasse J, de Billy F, Camut S, Truchet G . Correlation between ultrastructural differentiation of bacteroids and nitrogen fixation in alfalfa nodules. J Bacteriol. 1990; 172(8):4295-306. PMC: 213254. DOI: 10.1128/jb.172.8.4295-4306.1990. View

3.
Vitale A, Chrispeels M . Sorting of proteins to the vacuoles of plant cells. Bioessays. 1992; 14(3):151-60. DOI: 10.1002/bies.950140303. View

4.
Konami Y, Yamamoto K, Osawa T, Irimura T . Correlation between carbohydrate-binding specificity and amino acid sequence of carbohydrate-binding regions of Cytisus-type anti-H(O) lectins. FEBS Lett. 1992; 304(2-3):129-35. DOI: 10.1016/0014-5793(92)80603-e. View

5.
Chawla D, Animashaun T, Hughes R, Harris A, Aitken A . Bowringia mildbraedii agglutinin: polypeptide composition, primary structure and homologies with other legume lectins. Biochim Biophys Acta. 1993; 1202(1):38-46. DOI: 10.1016/0167-4838(93)90060-5. View