title: Glycoproteome of elongating cotton fiber cells.
abstract: Cotton ovule epidermal cell differentiation into long fibers primarily depends on wall-oriented processes such as loosening, elongation, remodeling, and maturation. Such processes are governed by cell wall bound structural proteins and interacting carbohydrate active enzymes. Glycosylation plays a major role in the structural, functional, and localization aspects of the cell wall and extracellular destined proteins. Elucidating the glycoproteome of fiber cells would reflect its wall composition as well as compartmental requirement, which must be system specific. Following complementary proteomic approaches, we have identified 334 unique proteins comprising structural and regulatory families. Glycopeptide-based enrichment followed by deglycosylation with PNGase F and A revealed 92 unique peptides containing 106 formerly N-linked glycosylated sites from 67 unique proteins. Our results showed that structural proteins like arabinogalactans and carbohydrate active enzymes were relatively more abundant and showed stage- and isoform-specific expression patterns in the differentiating fiber cell. Furthermore, our data also revealed the presence of heterogeneous and novel forms of structural and regulatory glycoproteins. Comparative analysis with other plant glycoproteomes highlighted the unique composition of the fiber glycoproteome. The present study provides the first insight into the identity, abundance, diversity, and composition of the glycoproteome within single celled cotton fibers. The elucidated composition also indirectly provides clues about unicellular compartmental requirements underlying single cell differentiation.
authors.affiliation: Plant Transformation Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), New Delhi, India;
authors.forename: Saravanan
authors.initials: S
authors.lastname: Kumar
authors.forename: Krishan
authors.initials: K
authors.lastname: Kumar
authors.forename: Pankaj
authors.initials: P
authors.lastname: Pandey
authors.forename: Vijayalakshmi
authors.initials: V
authors.lastname: Rajamani
authors.forename: Kethireddy Venkata
authors.initials: KV
authors.lastname: Padmalatha
authors.forename: Gurusamy
authors.initials: G
authors.lastname: Dhandapani
authors.forename: Mogilicherla
authors.initials: M
authors.lastname: Kanakachari
authors.forename: Sadhu
authors.initials: S
authors.lastname: Leelavathi
authors.forename: Polumetla Ananda
authors.initials: PA
authors.lastname: Kumar
authors.forename: Vanga Siva
authors.initials: VS
authors.lastname: Reddy
mesh_terms: D000595:Amino Acid Sequence; D002454:Cell Differentiation; D002473:Cell Wall / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D032561:Cotton Fiber; D004591:Electrophoresis, Polyacrylamide Gel; D018507:Gene Expression Regulation, Developmental; D018506:Gene Expression Regulation, Plant; D054794:Glycomics; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D006031:Glycosylation; D003368:Gossypium / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D058977:Molecular Sequence Annotation; D008969:Molecular Sequence Data; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / Q000737:chemistry; D059828:Plant Cells / Q000737:chemistry* / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D040901:Proteomics; D059010:Single-Cell Analysis; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D006023:Glycoproteins; D010940:Plant Proteins; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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