Repetitive proline-rich proteins in the extracellular matrix of the plant cell

Marcus, Abraham; Greenberg, Jonathan; Averyhart-Fullard, Vera

doi:10.1034/j.1399-3054.1991.810221.x

Cited by 16 publications

(23 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, Douglas fir (Pseudotsuga menziesii) Pro-rich HRGP is a PRP that undergoes arabinosylation only on contiguous Hyp residues, while the major peptide repeat motif also contains noncontiguous Hyp/Pro residues that are clustered yet remain nonglycosylated ( that also contains clustered noncontiguous Hyp, with only four amino acids separating the Hyp residues that also remain nonglycosylated (Marcus et al, 1991); maize THRGP possesses Thr-Hyp-Ser-Hyp repeats that undergo arabinosylation only; some dicot extensins, like tomato P1, also contain loosely clustered noncontiguous Hyp/Pro residues that are never arabinogalactosylated: Ser-Hyp 4 -Thr-Hyp-Val-Tyr-LysSer-Hyp 4 -Val-Lys-Pro-Tyr-His-Pro-Thr-Hyp-Val-Tyr-Lys. Why?…”

Section: Why Are Prps Not Glycosylated Like Agps?mentioning

confidence: 99%

Role of the Extensin Superfamily in Primary Cell Wall Architecture

et al. 2011

View full text Add to dashboard Cite

Section: Why Are Prps Not Glycosylated Like Agps?mentioning

confidence: 99%

Role of the Extensin Superfamily in Primary Cell Wall Architecture

et al. 2011

View full text Add to dashboard Cite

“…More than three decades after the discovery of Hyp as a constituent amino acid of cell wall polypeptides, the potential functions of each of the severa1 distinct classes of Hyp-rich proteins, glycoproteins, and proteoglycans remain speculative (Fincher et al, 1983;Cassab and Vamer, 1988;Vamer and Lin, 1989;Roberts, 1990;Marcus et al, 1991;Showalter, 1993). We used a selective inhibitor of prolyl hydroxylase, Dhp, to investigate the function of HRGPs synthesized during cell wall regeneration by tobacco mesophyll protoplasts.…”

Section: Functional Significance Of Hrcpsmentioning

confidence: 99%

“…To date, four distinct classes of Hyp-containing wall polymers have been described (extensins, AGPs, RPRPs, and Solanaceae lectins). Structural Hyp-containing proteins, glycoproteins, and proteoglycans may be important in controlling cell growth, cell differentiation, and disease resistance, but the precise molecular role(s) of any of these polymers in wall structure remains speculative (see Vamer and Lin, 1989;Roberts, 1990;Marcus et al, 1991;Showalter, 1993, for reviews).…”

mentioning

confidence: 99%

3,4-Dehydroproline Inhibits Cell Wall Assembly and Cell Division in Tobacco Protoplasts

1994

View full text Add to dashboard Cite

We investigated the function of cell wall hydroxyproline-rich glycoproteins by observing the effects of a selective inhibitor of prolyl hydroxylase, 3,4-dehydro-i-proline (Dhp), on wall regeneration by Nicofiana fabacum mesophyll cell protoplasts. Protoplasts treated with micromolar concentrations of Dhp do not develop osmotic stability and do not initiate mitosis. l h e architecture of regenerated cell walls was examined using deep-etch, freezefracture electron microscopy of rapidly frozen tobacco cells. Untreated protoplasts assemble a dense fibrillar cell wall consisting of laterally associating subelementary fibrils. In contrast, treatment of protoplasts with Dhp alters the structure of the regenerated wall fibrils in severa1 ways: first, the microfibrils are coated with globular knobs; second, some larger fiber bundles have an open ribbonlike appearance; and third, the smallest subelementary fibrils were not visible. Tobacco cells develop an abnormal morphology as a consequence of this abnormal cell wall structure. Thus, inhibition of prolyl hydroxylase results in the regeneration of a cell wall with abnormal structural and functional properties. These data provide experimental evidence that hydroxyproline-rich glycoproteins are important for the structural integrity of primary cell walls and for the correct assembly of other wall polymers, and that wall structure is an important regulator of cell division and cell morphology.The cell wall is a complex composite layer constructed of polysaccharides, proteins, and proteoglycans that surround the plasma membrane of plant cells. The tensile strength of the wall is thought to be provided by cellulose fibrils to which a xyloglucan gel is specifically hydrogen bonded. These gelcoated fibers are embedded in an independent gel matrix composed of neutra1 and acidic polysaccharides and structural proteins and glycoproteins. To date, four distinct classes of Hyp-containing wall polymers have been described (extensins, AGPs, RPRPs, and Solanaceae lectins). Structural Hyp-containing proteins, glycoproteins, and proteoglycans may be important in controlling cell growth, cell differentiation, and disease resistance, but the precise molecular role(s) of any of these polymers in wall structure remains speculative (see Vamer and

show abstract

“…ity that RPRP1, which is exclusively (Pro-Hyp-Val-Tyr-Lys)" (20,21), may be cross-linked in muro (21) (12). However, judging from CD spectra (Fig.…”

Section: Hhrgp In the Maize Mediummentioning

confidence: 99%

A Histidine-Rich Extensin from Zea mays Is an Arabinogalactan Protein

Kieliszewski

Kamyab²,

Leykam³

et al. 1992

Plant Physiol.

View full text Add to dashboard Cite

Earlier we isolated a threonine-rich extensin from maize (Zea mays). Here, we report that maize cell suspension cultures yield a new extensin rich in histidine (HHRGP) that also has characteristics of arabinogalactan proteins (AGPs). Thus, chymotryptic peptide maps of anhydrous hydrogen fluoride (HF)-deglycosylated HHRGP showed repetitive motifs related to both extensins and AGPs as follows. HHRGP contains Ala-Hyp3 and Ala-Hyp4 repeats that may be related to the classical dicot Ser-Hyp4 extensin motif by the single T -* G (Ser --Ala) base change. Furthermore, HHRGP also contains the repetitive motif Ala-Hyp-Hyp-HypHis-Phe-Pro-Ser-Hyp-Hyp related to the Ser-Hyp4-Ser-Hyp-SerHyp4 motif of P3-type dicot extensin. However, HHRGP also has AGP characteristics, notably an elevated alanine content, near sequence identity with the known Lo/ium AGP peptide Ser-HypHyp-Ala-Pro-Ala-Pro, the putative presence of glucuronoarabinogalactan, and precipitation by Yariv antigen, but fl-elimination of arabinogalactan indicates its 0-linkage to serine rather than the characteristic 0-hydroxyproline link of other AGPs. Although HHRGP might be a "chimera" of two different proteins, i.e. an extensin and an AGP, this is unlikely because one can account for the apparent chimera by the codon relationships of the five common hydroxyproline-rich glycoprotein amino acid residues, Ser, Pro, Thr, Ala (TCx, CCx, ACx, GCx) and histidine (CAT or CAC), which facilitate interconversion of major motifs by single point mutations. Thus, we propose that the extensin family of wall proteins consists of a highly diversified phylogenetic series ranging from basic minimally glycosylated repetitive pro-rich proteins to the highly glycosylated acidic AGPs. To relate this diversity of form and function at the molecular level, we identified putative functional domains hypothetically involved in properties such as reptation, recognition, adhesion, intermolecular cross-linkage, and self-assembly. herbaceous dicots whose walls are often rich in extensins: rodlike HRGPs,2 generally highly basic and consisting of variably glycosylated repetitive peptide motifs (8, 13-18, 30, 31, 34 Recently, we characterized a graminaceous monocot HRGP homologous with dicot extensins (12, 14, 15) but with some significant modifications. Here, we report the isolation of a second HRGP from the graminaceous monocot, Zea mays. This HRGP is unusually rich in His, hence an HHRGP, and is an apparent extensin AGP "chimera," i.e. it shares sequence homology and glycosylation patterns with both extensins (17,18,30,31,34) and AGPs (7,9,24). However, we suggest that HHRGP is not a chimera oftwo different proteins per se but, instead, occupies an intermediate position between extremes of the extensin family whose members are a phylogenetic series ranging from highly repetitive basic minimally glycosylated RPRPs to the highly glycosylated acidic AGPs. MATERIALS AND METHODS Suspension CulturesWe grew maize (Zea mays) cell suspensions (cv Black Mexican) in 1-L flasks containing 500 mL Muras...

show abstract

Repetitive proline-rich proteins in the extracellular matrix of the plant cell

Cited by 16 publications

References 0 publications

Role of the Extensin Superfamily in Primary Cell Wall Architecture

Role of the Extensin Superfamily in Primary Cell Wall Architecture

3,4-Dehydroproline Inhibits Cell Wall Assembly and Cell Division in Tobacco Protoplasts

A Histidine-Rich Extensin from Zea mays Is an Arabinogalactan Protein

Contact Info

Product

Resources

About