-
Molecular cloning of two cysteine proteinases from paw-paw (Carica papaya).
Two cDNA clones for plant cysteine proteinases have been isolated from a Carica papaya (paw-paw, papaya) leaf tissue cDNA library by using a mixture of 16 synthetic oligodeoxyribonucleotides as a hybridization probe. The inserted regions are 311 and 440 base-pairs in length and have the potential to encode a region corresponding to the C-terminal region of two proteins which are homologous with the known plant cysteine proteinases and the mammalian thiol cathepsins. One of the sequences shows a high (greater than 77%) homology with the plant cysteine proteinase papain, the other is closely related to papaya chymopapain. One sequence contains all, and the other most, of the 3' untranslated region of the mRNA. The inserts were used as specific probes in Northern Blot analyses giving an estimated size for the two mRNA species of 1.45 kilobases.
PMID: 3541893 [PubMed - indexed for MEDLINE]
PMCID: PMC1146953
-
Cited by 4 PubMed Central articles
-
Immunolocalization of a cysteine protease in vacuoles, vesicles, and symbiosomes of pea nodule cells.
Vincent JL, Brewin NJ.
Plant Physiol. 2000 Jun; 123(2):521-30.
[Plant Physiol. 2000]
-
Analysis of the prtP gene encoding porphypain, a cysteine proteinase of Porphyromonas gingivalis.
Barkocy-Gallagher GA, Han N, Patti JM, Whitlock J, Progulske-Fox A, Lantz MS.
J Bacteriol. 1996 May; 178(10):2734-41.
[J Bacteriol. 1996]
-
Cloning and characterization of a new protease gene (prtH) from Porphyromonas gingivalis.
Fletcher HM, Schenkein HA, Macrina FL.
Infect Immun. 1994 Oct; 62(10):4279-86.
[Infect Immun. 1994]
- » See all...