The Experts below are selected from a list of 34683 Experts worldwide ranked by ideXlab platform
Bandar A Suliman - One of the best experts on this subject based on the ideXlab platform.
-
the promyelocytic leukemia Zinc Finger Protein two decades of molecular oncology
Frontiers in Oncology, 2012Co-Authors: Bandar A Suliman, Dakang Xu, Bryan R G WilliamsAbstract:The promyelocytic leukemia Zinc Finger Protein (PLZF), also known as Zbtb16 or Zfp145, was first identified in a patient with acute promyelocytic leukemia, where a reciprocal chromosomal translocation t(11;17)(q23;q21) resulted in a fusion with the RARA gene encoding retinoic acid receptor alpha. The wild-type Zbtb16 gene encodes a transcription factor that belongs to the POK (POZ and Kruppel) family of transcriptional repressors. In addition to nine Kruppel-type sequence-specific Zinc Fingers, which make it a member of the Kruppel-like Zinc Finger Protein family, the PLZF Protein contains an N-terminal BTB/POZ domain and RD2 domain. PLZF has been shown to be involved in major developmental and biological processes, such as spermatogenesis, hind limb formation, hematopoiesis, and immune regulation. PLZF is localized mainly in the nucleus where it exerts its transcriptional repression function, and many post-translational modifications affect this ability and also have an impact on its cytoplasmic/nuclear dissociation. PLZF achieves its transcriptional regulation by binding to many secondary molecules to form large multi-Protein complexes that bind to the regulatory elements in the promoter region of the target genes. These complexes are also capable of physically interacting with its target Proteins. Recently, PLZF has become implicated in carcinogenesis as a tumor suppressor gene, since it regulates the cell cycle and apoptosis in many cell types. This review will examine the major advances in our knowledge of PLZF biological activities that augment its value as a therapeutic target, particularly in cancer and immunological diseases.
Hongsheng Zhang - One of the best experts on this subject based on the ideXlab platform.
-
functional analysis of a novel cys2 his2 type Zinc Finger Protein involved in salt tolerance in rice
Journal of Experimental Botany, 2010Co-Authors: Shujing Sun, Ji Huang, Xia Yang, Haijuan Tang, Shuqiao Guo, Yongmei Bao, Hui Sun, Hongsheng ZhangAbstract:The Cys2/His2-type Zinc Finger Proteins have been implicated in different cellular processes involved in plant development and stress responses. Through microarray analysis, a salt-responsive Zinc Finger Protein gene ZFP179 was identified and subsequently cloned from rice seedlings. ZFP179 encodes a 17.95 kDa Protein with two C2H2-type Zinc Finger motifs having transcriptional activation activity. The real-time RT-PCR analysis showed that ZFP179 was highly expressed in immature spikes, and markedly induced in the seedlings by NaCl, PEG 6000, and ABA treatments. Overexpression of ZFP179 in rice increased salt tolerance and the transgenic seedlings showed hypersensitivity to exogenous ABA. The increased levels of free proline and soluble sugars were observed in transgenic plants compared to wild-type plants under salt stress. The ZFP179 transgenic rice exhibited significantly increased tolerance to oxidative stress, the reactive oxygen species (ROS)-scavenging ability, and expression levels of a number of stress-related genes, including OsDREB2A, OsP5CS OsProT, and OsLea3 under salt stress. Our studies suggest that ZFP179 plays a crucial role in the plant response to salt stress, and is useful in developing transgenic crops with enhanced tolerance to salt stress.
-
Cloning and expression analysis of ZFP207 encoding a TFIIIA-type Zinc Finger Protein in rice
Hereditas (beijing), 2010Co-Authors: Fan-jun Meng, Ji Huang, Yan Jiang, Hongsheng ZhangAbstract:The Zinc finer Proteins consist of a large transcription factor family involved in plant development and responses to environmental stresses.In this paper,a TFⅢA-type Zinc Finger Protein gene ZFP207(GenBank assession number AK063147.1)was cloned from rice variety Jiucaiqing by RT-PCR approach.This gene contains an open reading frame (ORF)of 567 bp,which encodes a peptide of 188 amino acid residues.The isoelectric point(pI)of the Protein is 9.67,and its molecular weight is 20.72 kDa.Bioinformatic analysis showed that the ZFP207 Protein comprises a typical TF ⅢA-type Zinc Finger domain and an EAR-motif at its C-terminus.However,nuclear localization signals(NLS)commonly existing in TFⅢA-type Zinc Finger Proteins was not found in the ZFP207 amino acid sequence.In addition,based on the alignments of the whole amino acid sequences of some known TFⅢA-type Zinc Finger Proteins in plants,a phylogenetic tree was constructed by the neighbour joining method.The phylogenetic tree showed that ZFP207 and other TFⅢA-type Zinc Finger Proteins with single Zinc Finger domain were grouped into the same branch.The expression pattern of ZFP207 gene was also investigated in various rice tissues at adult stage by RT-PCR and the results showed that ZFP207 was expressed with high levels in culms and leaves,but lower in roots and spikes.Finally,the trans-activation assay in yeast cells revealed that ZFP207 lacked the trans-activation activity.
-
overexpression of a tfiiia type Zinc Finger Protein gene zfp252 enhances drought and salt tolerance in rice oryza sativa l
FEBS Letters, 2008Co-Authors: Dongqing Xu, Ji Huang, Xia Yang, Haijuan Tang, Hongsheng ZhangAbstract:We previously identified a salt and drought stress-responsive TFIIIA-type Zinc Finger Protein gene ZFP252 from rice. Here we report the functional analysis of ZFP252 using gain- and loss-of-function strategies. We found that overexpression of ZFP252 in rice increased the amount of free proline and soluble sugars, elevated the expression of stress defense genes and enhanced rice tolerance to salt and drought stresses, as compared with ZFP252 antisense and non-transgenic plants. Our findings suggest that ZFP252 plays an important role in rice response to salt and drought stresses and is useful in engineering crop plants with enhanced tolerance to salt and drought stresses.
Bryan R G Williams - One of the best experts on this subject based on the ideXlab platform.
-
the promyelocytic leukemia Zinc Finger Protein two decades of molecular oncology
Frontiers in Oncology, 2012Co-Authors: Bandar A Suliman, Dakang Xu, Bryan R G WilliamsAbstract:The promyelocytic leukemia Zinc Finger Protein (PLZF), also known as Zbtb16 or Zfp145, was first identified in a patient with acute promyelocytic leukemia, where a reciprocal chromosomal translocation t(11;17)(q23;q21) resulted in a fusion with the RARA gene encoding retinoic acid receptor alpha. The wild-type Zbtb16 gene encodes a transcription factor that belongs to the POK (POZ and Kruppel) family of transcriptional repressors. In addition to nine Kruppel-type sequence-specific Zinc Fingers, which make it a member of the Kruppel-like Zinc Finger Protein family, the PLZF Protein contains an N-terminal BTB/POZ domain and RD2 domain. PLZF has been shown to be involved in major developmental and biological processes, such as spermatogenesis, hind limb formation, hematopoiesis, and immune regulation. PLZF is localized mainly in the nucleus where it exerts its transcriptional repression function, and many post-translational modifications affect this ability and also have an impact on its cytoplasmic/nuclear dissociation. PLZF achieves its transcriptional regulation by binding to many secondary molecules to form large multi-Protein complexes that bind to the regulatory elements in the promoter region of the target genes. These complexes are also capable of physically interacting with its target Proteins. Recently, PLZF has become implicated in carcinogenesis as a tumor suppressor gene, since it regulates the cell cycle and apoptosis in many cell types. This review will examine the major advances in our knowledge of PLZF biological activities that augment its value as a therapeutic target, particularly in cancer and immunological diseases.
Jeremy M Berg - One of the best experts on this subject based on the ideXlab platform.
-
DNA UNWINDING INDUCED BY Zinc Finger Protein BINDING
Biochemistry, 1996Co-Authors: Jeremy M BergAbstract:Zinc Finger domains of the Cys2His2 type are found in a large number of eukaryotic Proteins. Various Proteins containing these domains have been shown to bind specifically to DNA, RNA, and DNA-RNA hybrids. Structural studies of Zinc Finger Protein-DNA complexes have revealed that the DNA molecules are underwound relative to canonical B-form. It has not been clear if Zinc Finger Proteins recognize preexisting underwound conformations of DNA or if they induce such conformations upon binding. We report that the DNA binding domains of Sp1 and several designed Zinc Finger Proteins unwind DNA upon binding. The extent of unwinding is consistent with that observed in Zinc Finger Protein-DNA cocrystal structures. These DNA deformations may be important in determining overall binding affinities as well as influencing binding site preferences. Furthermore, changes in DNA conformation upon Zinc Finger Protein binding may affect Protein-Protein interactions important for transcriptional regulation and other activities of Zinc Finger Proteins.
-
toward rules relating Zinc Finger Protein sequences and dna binding site preferences
Proceedings of the National Academy of Sciences of the United States of America, 1992Co-Authors: John R Desjarlais, Jeremy M BergAbstract:Abstract Zinc Finger Proteins of the Cys2-His2 type consist of tandem arrays of domains, where each domain appears to contact three adjacent base pairs of DNA through three key residues. We have designed and prepared a series of variants of the central Zinc Finger within the DNA binding domain of Sp1 by using information from an analysis of a large data base of Zinc Finger Protein sequences. Through systematic variations at two of the three contact positions (underlined), relatively specific recognition of sequences of the form 5'-GGGGN(G or T)GGG-3' has been achieved. These results provide the basis for rules that may develop into a code that will allow the design of Zinc Finger Proteins with preselected DNA site specificity.
-
redesigning the dna binding specificity of a Zinc Finger Protein a data base guided approach
Proteins, 1992Co-Authors: John R Desjarlais, Jeremy M BergAbstract:: A peptide corresponding to the three Zinc Finger domains of the human transcription factor Sp1 has been expressed and found to bind a consensus Sp1 binding site with the sequence 5'-GGGGCGGGG-3'. Examination of the amino acid distributions within a large Zinc Finger sequence data base and chemical arguments suggested that a particular Arg to Gln sequence change might convert binding specificity to 5'-GGGGCAGGG-3'. Experimental tests of this hypothesis revealed that such a change could be induced only when two other sequence changes, deduced from examination of sequence correlations, were made as well. These results provide the most direct information to date about how Zinc Finger Proteins might recognize adenine-containing binding sites and bear on the existence and nature of any code between Zinc Finger Protein and binding site sequences.
N Mueller-lantzsch - One of the best experts on this subject based on the ideXlab platform.
-
Human endogenous retrovirus Protein cORF supports cell transformation and associates with the promyelocytic leukemia Zinc Finger Protein
Oncogene, 2000Co-Authors: A Boese, M Sauter, U Galli, B Best, H Herbst, J Mayer, E Kremmer, K Roemer, N Mueller-lantzschAbstract:Human endogenous retrovirus sequences (HERVs) reside in the genomes of primates and humans for several million years. The majority of HERVs is non-coding but a limited set is intact and can express Proteins. We have recently identified an almost intact HERV-K(HML-2) provirus on chromosome 7 and have documented that most patients with germ cell tumors (GCTs) display antibodies directed against Proteins of HERV-K(HML-2). To address whether these Proteins merely represent tumor markers or contribute to neoplastic transformation, we examined the transforming potential of various HERV sequences and studied physical interactions between HERV and cellular Proteins by yeast two-hybrid and biochemical assays. cORF, a Protein encoded by the C-terminal open reading frame within the env gene, supports tumor growth in nude mice and associates with the promyelocytic leukemia Zinc Finger Protein (PLZF). The interaction domains map between amino acid residues 21 and 87 of cORF, and between residues 245 and 543 of PLZF. PLZF is critical for spermatogenesis in mice. Abnormal spermatogenesis or maturation of gonocytes is thought to predispose humans to the development of germ cell tumors. Thus, cORF of human endogenous retroviruses may contribute to tumor development by interfering with processes during spermatogenesis that involve PLZF.
