scholarly journals Amino acid sequence of the coat protein subunit in satellite tobacco necrosis virus

1981 ◽  
Vol 152 (1) ◽  
pp. 171-179 ◽  
Author(s):  
D. Henriksson ◽  
R.J. Tanis ◽  
R.E. Tashian ◽  
P.O. Nyman
FEBS Letters ◽  
1978 ◽  
Vol 96 (2) ◽  
pp. 381-384 ◽  
Author(s):  
Blas Frangione ◽  
Yasutsugu Nakashima ◽  
William Konigsberg ◽  
Robert L. Wiseman

1967 ◽  
Vol 242 (15) ◽  
pp. 3563-3578
Author(s):  
Klaus Weber ◽  
William Konigsberg

1970 ◽  
Vol 67 (3) ◽  
pp. 403-413 ◽  
Author(s):  
TOHRU NISHIHARA ◽  
YUZO NOZU ◽  
YOSHIMI OKADA

Plant Disease ◽  
2004 ◽  
Vol 88 (5) ◽  
pp. 516-522 ◽  
Author(s):  
Gustavo Fermin ◽  
Valentina Inglessis ◽  
Cesar Garboza ◽  
Sairo Rangel ◽  
Manuel Dagert ◽  
...  

Local varieties of papaya grown in the Andean foothills of Mérida, Venezuela, were transformed independently with the coat protein (CP) gene from two different geographical Papaya ringspot virus (PRSV) isolates, designated VE and LA, via Agrobacterium tumefaciens. The CP genes of both PRSV isolates show 92 and 96% nucleotide and amino acid sequence similarity, respectively. Four PRSV-resistant R0 plants were intercrossed or selfed, and the progenies were tested for resistance against the homologous isolates VE and LA, and the heterologous isolates HA (Hawaii) and TH (Thailand) in greenhouse conditions. Resistance was affected by sequence similarity between the transgenes and the challenge viruses: resistance values were higher for plants challenged with the homologous isolates (92 to 100% similarity) than with the Hawaiian (94% similarity) and, lastly, Thailand isolates (88 to 89% similarity). Our results show that PRSV CP gene effectively protects local varieties of papaya against homologous and heterologous isolates of PRSV.


1972 ◽  
Vol 36 (7) ◽  
pp. 1109-1116 ◽  
Author(s):  
Kotoku KURACHI ◽  
Gunki FUNATSU ◽  
Masaru FUNATSU ◽  
Soh HIDAKA

1991 ◽  
Vol 119 (1-2) ◽  
pp. 25-35 ◽  
Author(s):  
N. M. McKern ◽  
H. K. Edskes ◽  
C. W. Ward ◽  
P. M. Strike ◽  
O. W. Barnett ◽  
...  

1966 ◽  
Vol 20 (2) ◽  
pp. 423-425 ◽  
Author(s):  
Klaus Weber ◽  
Gursuran Notani ◽  
Maurice Wikler ◽  
William Konigsberg

1992 ◽  
Vol 282 (2) ◽  
pp. 447-452 ◽  
Author(s):  
A L Newsome ◽  
J W McLean ◽  
M O Lively

Detergent-solubilized hen oviduct signal peptidase has been characterized previously as an apparent complex of a 19 kDa protein and a 23 kDa glycoprotein (GP23) [Baker & Lively (1987) Biochemistry 26, 8561-8567]. A cDNA clone encoding GP23 from a chicken oviduct lambda gt11 cDNA library has now been characterized. The cDNA encodes a protein of 180 amino acid residues with a single site for asparagine-linked glycosylation that has been directly identified by amino acid sequence analysis of a tryptic-digest peptide containing the glycosylated site. Immunoblot analysis reveals cross-reactivity with a dog pancreas protein. Comparison of the deduced amino acid sequence of GP23 with the 22/23 kDa glycoprotein of dog microsomal signal peptidase [Shelness, Kanwar & Blobel (1988) J. Biol. Chem. 263, 17063-17070], one of five proteins associated with this enzyme, reveals that the amino acid sequences are 90% identical. Thus the signal peptidase glycoprotein is as highly conserved as the sequences of cytochromes c and b from these same species and is likely to be found in a similar form in many, if not all, vertebrate species. The data also show conclusively that the dog and avian signal peptidases have at least one protein subunit in common.


1972 ◽  
Vol 127 (1) ◽  
pp. 167-178 ◽  
Author(s):  
D. T. Snell ◽  
R. E. Offord

1. Bacteriophage ZJ-2 is a filamentous male-specific coliphage. Methods are given for its preparation and separation into nucleic acid and the major coat-protein component (B-protein). 2. The determination of the amino acid sequence of the B-protein of bacteriophage ZJ-2 is described. The principal features of this aspect of the work were the special procedures dictated by the insolubility of the protein and the extreme insolubility of its fragments. The sequence is compared with that obtained by other workers for the coat protein of the related bacteriophage fd.


Sign in / Sign up

Export Citation Format

Share Document