Abstract:
:The cloning and analysis of a cDNA clone encoding the soybean metalloproteinase obtained by polymerase chain reaction (PCR) and the rapid amplification of cDNA ends (RACE) reaction are described. The cDNA was constructed from poly(A)+ RNA isolated from 15-17 day old leaves. The deduced amino acid sequence of the cDNA reveals that the plant metalloproteinase is synthesized as a preproenzyme and the proenzyme form shares a structural motif, responsible for maintenance of inactive zymogen, with the matrix metalloproteinase (e.g. collagenase) family of enzymes from vertebrate origin. Northern and Western blot analysis demonstrated that the metalloproteinase transcript and protein are under a strict developmental program in that both are expressed only in leaf tissue and in a temporal fashion. The physiological function of the metalloproteinase still remains unclear although the data suggest that the enzyme is extracellular and a portion of the mature form of the enzyme is tightly bound to the cell wall.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pak JH,Liu CY,Huangpu J,Graham JSdoi
10.1016/s0014-5793(97)00141-5subject
Has Abstractpub_date
1997-03-10 00:00:00pages
283-8issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00141-5journal_volume
404pub_type
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