ALBERT — All Library Books, journals and Electronic Records Telegrafenberg

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

MtENOD16 and 20 are members of a family of phytocyanin-related early nodulins (1998)

Greene, Elizabeth A. ; Erard, Monique ; Dedieu, Annie ; [et al.]

Springer

Plant molecular biology 36 (1998), S. 775-783

add to mindlist on the mindlist

Details

ISSN: 1573-5028

Keywords: early nodulin ; Medicago truncatula ; molecular modelling ; phytocyanin ; proline-rich protein ; symbiosis

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract We have identified two single-copy genes from the model legume Medicago truncatula (MtENOD16 and 20) whose expression can be correlated with early stages of root nodulation and whose predicted coding sequences are partially homologous to both pea/vetch ENOD5 and soybean N315/ENOD55. Database searching and sequence alignment have defined the encoded early nodulins as a distinct sub-family of phytocyanin-related proteins, although the absence of key ligands implies that they are unlikely to bind copper. Molecular modelling based on known phytocyanin structure has been used to predict the 3-dimensional conformation of the principle globular domain of MtENOD16/20. Additional structural features common to both early nodulin and phytocyanin precursors include an N-terminal transit peptide, a highly variable (hydroxy)proline-rich sequence which probably undergoes extensive post-translational modification, and a hydrophobic C-terminal tail.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1005916821224

Permalink

	Location	Call Number	Expected	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

A covalently cross-linked matrix in skeletal muscle fibers (1983)

Loewy, Ariel G. ; Wilson, Frank J. ; Taggart, Nina M. ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 3 (1983), S. 463-483

add to mindlist on the mindlist

Details

ISSN: 0886-1544

Keywords: intracellular matrix ; extracellular matrix ; covalently cross-linked matrix ; ε-(γ-glutamic) lysine bonds ; skeletal muscle ; titin ; covalently cross-linked collagen ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: When skeletal, cardiac, and smooth muscle is exhaustively extracted with a protein-unfolding reagent such as 6 M guanidine HCl and a disulfide-reducing reagent such as 5% β-mercaptoethanol, a tissue ghost remains intact and retains the characteristic shape and dimensions of the tissue before extraction. In the case of chicken pectoral muscle, the tissue ghost contains 1% of the original muscle proteins. Guanidine HCl extraction followed by collagenase treatment of glycerol-extracted chicken pectoral muscle releases a clean preparation of elongated structures containing 0.2% of the original protein and representing the covalently cross-linked remnants of the muscle fibers. The material of these muscle fiber ghosts extends throughout the interior of the cell. Antibodies raised against the tissue ghosts of smooth muscle cross-react with glycerol extracted skeletal myofibrils, forming a banding pattern which coincides with the banding pattern observed when myofibrils are reacted with antibodies against titin. Titin, a large and soluble protein found in skeletal muscle, cross-reacts with our antigizzard antibody. However, amino acid analysis of the muscle fiber ghosts indicates that titin cannot be the only subunit of the insoluble polymer, but that one or more proteins with a very high glycine and alanine content and a very low basic and acidic amino acid content must also form part of the covalently cross-linked matrix. The possibility is presented that this matrix may be the basis of the superthin 2-3-nm filaments which have been observed in a variety of cell types.

Additional Material: 12 Ill.