Mutant Name: cyt1 (emb101)
| Gene Name | CYT1 |
| Protein Name | GDP-mannose pyrophosphorylase |
| Mutagen | T-DNA |
| Category | forward genetics |
| Organism | Arabidopsis thaliana |
| Ecotype | Ws |
| Donor | |
| General Description |
1.Mutants were embryonic lethal resulting from both a disruption of cytokinesis and a failure to synthesize a normal cell wall. 2.Mutants showed radial swelling, excessive cell-wall thickenings, and inappropriate callose accumulation. 3.The cyt1-1 allele had a point mutation in codon 89 (CCT to CTT) resulting in a change from proline to leucine. In the cyt1-2 allele a single nucleotide was inserted in codon 306 (TCG to TTCG) causing a 1 frameshift and at the same time disrupting an XhoI site. 4.A weak mutation in the same gene, vtc1, was previously isolated because of its low content of ascorbic acid. |
| Organ Specificity | CYT1 transcripts were about 1.5 kb in size and expressed in all tissues examined (seedlings, roots, leaves, stems, inflorescences) |
| Impact on Wall |
1. thickened cell walls resulting from massive accumulation of PAS-positive polysaccharides. 2. Inappropriate callose formation in both intact and incomplete cell walls; 3. diffuse localization of unesterified pectins throughout the cell wall. |
| Impact on Sugar Composition |
1.The cell walls of cyt1-1 embryos contained reduced amounts of mannose (35% of wild-type) and fucose (45% of wild-type). Other noticeable differences were elevated levels of rhamnose (152% of wild-type) and xylose (122% of wild-type). 2.Mutant cyt1 embryos are deficient in N-glycosylation . Most notably, they show a 5-fold decrease in cellulose content. 3.excessive callose accumulation in root. |
| Reference |
1.Todd C. Nickle and David W. Meinke.A cytokinesis-defective mutant of Arabidopsis ( cyt1 ) characterized by embryonic lethality, incomplete cell walls, and excessive callose accumulation.The Plant Journal.(1998)15(3),321-332 2.Lukowitz W, Nickle TC, Meinke DW, Last RL, Conklin PL, Somerville CR. Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate guanylyltransferase and point to a requirement of N-linked glycosylation for cellulose biosynthesis.Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2262-7. |