Analysis of the amino acid sequences of plant Bowman-Birk inhibitors

Prakash, Balaji; Selvaraj, Samuel; Murthy, M.R.N.; Sreerama, Y. N.; Rao, D. Rajagopal; Gowda, Lalitha R.

doi:10.1007/bf02352286

Cited by 103 publications

(71 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In contrast, the 16-kD inhibitors have two homologous BBI domains with one reactive site in each domain. It is therefore thought that the 16-kD inhibitors evolved from the monocotyledonous 8-kD single-headed inhibitors (Prakash et al, 1996).…”

mentioning

confidence: 99%

Molecular Cloning and Functional Analysis of a Novel Type of Bowman-Birk Inhibitor Gene Family in Rice

et al. 2003

View full text Add to dashboard Cite

inhibitor (BBI) genes encode serine protease inhibitors that have repetitive cysteine-rich domains with reactive sites for the trypsin or chymotrypsin family. We have identified seven BBI genes from japonica rice (Oryza sativa subsp. japonica var Teqing). All of the genes identified were found in a single cluster on the southern end of the long arm of rice chromosome 1. Four of the seven BBI genes have two repetitive cysteine-rich domains, whereas one has a truncated domain with only one reactive site. We have also identified three novel BBI genes, each of which possesses three repetitive domains instead of two. In situ hybridization analyses indicated that the accumulation of rice BBI transcripts was differentially regulated in germinating embryos and also in the leaves, roots, and flower organs at later developmental stages. Different members of the rice BBI gene family displayed different expression patterns during rice seed germination, and wounding induced the expression of rice BBI transcripts. The three-domain BBIs had higher expression levels than the two-domain BBIs. It was also found that the mRNA of rice BBI genes was present in abundant amounts in scutellar epithelium and aleurone layer cells. RBBI3-1, one of the three-domain RBBI, exhibited in vitro trypsin-inhibiting activity but no chymotrypsin-inhibiting activity. Overexpression of RBBI2-3 in transgenic rice plants resulted in resistance to the fungal pathogen Pyricularia oryzae, indicating that proteinase inhibitors confer resistance against the fungal pathogen in vivo and that they might play a role in the defense system of the rice plant.Plants have developed defense systems to combat various pathogens throughout their life cycle, from the seed stage until senescence, and it is particularly important that the embryo be kept free from infection. There are several embryonic defense mechanisms, including the production of plant lectins and pathogen-related proteins in response to attacks by pathogens or insects (Swegle et al., 1992;Ye et al., 2001;Guiderdoni et al., 2002). A well-known defense component is Ser protease inhibitors. They are expressed in developing seeds and are thought to play an important role in inhibiting trypsin and chymotrypsin of external origin (Ryan, 1981). Two major Ser protease inhibitors have been studied extensively in plants: Kunitz inhibitors and Bowman-Birk inhibitors (BBIs; Ryan, 1990). BBIs are Cys-rich proteins of about 8 to 16 kD with disulfide bonds and are encoded by a family of related genes. The BBI gene family has been found in both the Fabaceae and the Poaceae. BBIs identified in Fabaceae, such as soybean (Glycine max) and lima bean (Phaseolus lunatus), are 8-kD proteins. They have one BBI domain with two reactive sites for trypsin and the related enzymes, such as chymotrypsin (Birk, 1987). These protease inhibitors are double-headed, with two reactive sites in a single inhibitor molecule. Interestingly, this type of inhibitor displays anticarcinogenic activity (Birk, 1993;Kennedy, 1993).The BBIs found in...

show abstract

mentioning

confidence: 99%

Molecular Cloning and Functional Analysis of a Novel Type of Bowman-Birk Inhibitor Gene Family in Rice

et al. 2003

View full text Add to dashboard Cite

show abstract

“…The growing interest of protein mimicking coupled with use of natural scaffolds as templates and capacity for diversity in chemical synthesis has resulted in an enormous number of synthetic peptide mimics 31,33,40,41 . Horsegram seed HGI-III consists of two similar domains each displaying heterologous anti-proteinase activity 42 . The seed HGI-III inhibits trypsin with a K i of 87 nM.…”

Section: Discussionmentioning

confidence: 99%

Molecular engineering of a small trypsin inhibitor based on the binding loop of horsegram seed Bowman-Birk inhibitor

Muricken

Gowda

2010

Journal of Enzyme Inhibition and Medicinal Chemistry

Self Cite

View full text Add to dashboard Cite

“…Cajanus indicus) [125][126][127][128][129][130][131][132][133][134][135][136][137][138][139][140]. It has been found as an effective chemopreventive agent against prostate cancer in animal models by blocking the generation of reactive oxygen species in prostate cancer cells [141].…”

Section: Bowmam-birk Protease Inhibitors (Bbi)mentioning

confidence: 99%