scholarly journals Role of nodD gene product and flavonoid interactions in induction of nodulation genes in Mesorhizobium ciceri

2010 ◽  
Vol 16 (1) ◽  
pp. 69-77 ◽  
Author(s):  
D. V. Kamboj ◽  
Ranjana Bhatia ◽  
D. V. Pathak ◽  
P. K. Sharma
1991 ◽  
pp. 115-136 ◽  
Author(s):  
Adam Kondorosi ◽  
Eva Kondorosi ◽  
Michael John ◽  
Jürgen Schmidt ◽  
Jeff Schell

1984 ◽  
Vol 158 (1) ◽  
pp. 187-194 ◽  
Author(s):  
J Imperial ◽  
R A Ugalde ◽  
V K Shah ◽  
W J Brill

2008 ◽  
Vol 73 (9) ◽  
pp. 995-999
Author(s):  
L. P. Kurochkina ◽  
A. Yu. Vishnevskiy ◽  
V. V. Mesyanzhinov

1987 ◽  
Vol 6 (4) ◽  
pp. 841-848 ◽  
Author(s):  
Beatrix Horvath ◽  
Christian W.B. Bachem ◽  
Jeff Schell ◽  
Adam Kondorosi

Cell ◽  
1982 ◽  
Vol 31 (1) ◽  
pp. 285-292 ◽  
Author(s):  
Gary Struhl ◽  
Danny Brower
Keyword(s):  

Microbiology ◽  
2006 ◽  
Vol 152 (11) ◽  
pp. 3383-3389 ◽  
Author(s):  
E. Vanterpool ◽  
F. Roy ◽  
W. Zhan ◽  
S. M. Sheets ◽  
L. Sangberg ◽  
...  

The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein–protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.


Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 3365-3365
Author(s):  
Jean-Yves Metais ◽  
Ashley E. Dunfee ◽  
Rodrigo T. Calado ◽  
Cynthia E. Dunbar

Abstract We recently reported development of an acute myeloid leukemia in a rhesus macaque transplanted with autologous CD34+ cells transduced with a murine stem cell virus-derived replication defective retrovirus vector expressing only marker genes under control of the strong MCSV LTR. This animal had an unusual clonal reconstitution pattern the first year following transplant, with a single transduced myeloid progenitor cell clone accounting for up to 80% of then normal myelopoiesis (Kelly, 2005). The same vector-containing clone then transformed to AML five years following transplantation, and each tumor cell was shown to contain two vector insertions, one localized 20 kb upstream the CDw92 gene on chromosome 9, and the second localized in the first intron of BCL2A1 on chromosome 15 (Seggewiss, 2006), a gene in the anti-apoptotic BCL2 family not previously linked to myeloid leukemia. BCL2A1 was highly expressed in the tumor cells. This tumor was the first hematopoietic malignancy reported in a recipient of primitive cells transduced with a replication-incompetent vector containing only marker genes, and suggested that BCL2A1 could have potent effects on myeloid cell behavior. To investigate the impact of the BCL2A1 gene product on hematopoietic cells, we cloned the murine and human HA-tagged BCL2A1 cDNAs into lentivirus vectors and transduced the murine BaF3 hematopoietic cell line as a model to study the impact of expression of these proteins on hematopoiesis. We confirmed overexpression of the proteins in the producer cell line as well as in transduced cells by western blot using an anti-HA monoclonal antibody. BaF3 cell proliferation and survival are dependant on IL-3, and under IL-3 replete conditions overexpression of murine or human BCL2A1 did alter proliferation compared with untransduced cells or cells transduced with an empty vector. Removal of IL-3 from the cell culture media leads to rapid apoptosis of BaF3 cells, with cell cycle arrest in the G1 and an apoptotic subpopulation appearing within 24 hours of IL-3 removal. 45% untransduced or empty vector cells were apoptotic, and this fraction decreased to 30% and 15% respectively for BaF3 cells expressing murine or human BCL2A1. These results were confirmed by direct analysis of apoptosis. Only BaF3 cells over-expressing human BCL2A1 were still alive and arrested in G1 after 3 days of culture without IL-3. The murine BCL2A1 had similar but less striking effects. Gene expression analyses on the BaF3 cell populations are ongoing, to identify potential downstream targets of the BCL2A1 protein. The BCL2A1 and empty vectors were also utilized in murine bone marrow cell immortalization assay, previously utilized to identify genes impacting on the survival and expansion of primary myeloid progenitor cells (Du, 2005). In an initial set of experiments, clonal clonal expansion was obtained with marrow cells expressing murine (4 clones) and human (5 clones) BCL2A1 but not for empty vector or untransduced murine marrow. Mice have also been transplanted with primary bone marrow cells transduced with the BCL2A1 and control vectors, and are being followed for in vivo expansion of transduced clones and development of leukemia. In conclusion, we have confirmed the role of BCL2A1 as an anti-apoptotic protein, now in myeloid hematopoietic cells, and will continue to investigate the role of this gene product in hematopoiesis and leukemogenesis.


Nature ◽  
1981 ◽  
Vol 290 (5806) ◽  
pp. 523-526 ◽  
Author(s):  
Harvey I. Miller ◽  
Howard A. Nash
Keyword(s):  

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