Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins

Fridell, Robert A.; Harding, Leslie S.; Bogerd, Hal P.; Cullen, Bryan R.

doi:10.1006/viro.1995.1266

Cited by 129HIV Research and TreatmentGenomics and Chromatin DynamicsHIV/AIDS drug development and treatment

Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins

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Fridell, Robert A., Harding, Leslie S., Bogerd, Hal P., Cullen, Bryan R.·1995·Virology

DOI 10.1006/viro.1995.1266

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Abstract

Transcriptional activation of HIV-1 gene expression by the viral Tat protein requires the interaction of a cellular cofactor with the Tat activation domain. This domain has been shown to consist of the cysteine-rich and core motifs of HIV-1 Tat and is functionally conserved in the distantly related Tat proteins of HIV-2 and EIAV. Using the yeast two-hybrid system, we have identified a novel human gene product, termed HT2A, that specifically and precisely binds to the activation domain of HIV-1 Tat and that can also interact with the HIV-2 and EIAV Tat proteins in vivo. We present data further demonstrating that the interaction between the activation domain of HIV-1 Tat and the HT2A protein can be readily detected in the mammalian cell nucleus. Sequence analysis demonstrates that HT2A is a novel member of the C3HC4 or ring finger family of zinc finger proteins that includes several known oncogenes and transcription factors. Overall, these data suggest that HT2A may play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo.

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TRIM32, previously known as HT2A, was originally discovered using a yeast two-hybrid assay with human immunodeficiency virus type 1 Tat as bait.
“It was originally discovered using a yeast two-hybrid assay with the human immunodeficiency virus type 1 Tat acting as bait (Fridell et al. 1995; Reymond et al. 2001).”
From Limb-Girdle Muscular Dystrophy Type 2H Associated with Mutation in TRIM32, a Putative E3-Ubiquitin–Ligase Gene (2002) · cites this paper as Fridell et al. 1995

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“TRIM32 was identified by yeast two-hybrid as a binding partner of HIV-1 Tat (Fridell et al. 1995) and has since been shown to target STING/MITA, the signal adaptor, for K63-linked”
Background
Inhibition of human immunodeficiency virus type 1 and type 2 Tat function by transdominant Tat protein localized to both the nucleus and cytoplasm
Orsini, M., & Debouck, C. M. (1996) · Journal of Virology · doi:10.1128/jvi.70.11.8055-8063.1996 · Cited by 31 · see citing works
“Recently, a cellular factor containing a zinc finger domain and homology to several oncogenes and transcription factors that interacts with Tat through both the core and cysteine-rich domains was identified (18).”
Background
TRIM-NHL as RNA Binding Ubiquitin E3 Ligase (RBUL): Implication in development and disease pathogenesis
Goyani, S., Roy, M., & Singh, R. K. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.166066 · Cited by 30 · see citing works
Epithelin/Granulin Growth Factors: Extracellular Cofactors for HIV-1 and HIV-2 Tat Proteins
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Trim32 Deficiency Enhances Th2 Immunity and Predisposes to Features of Atopic Dermatitis
Liu, Y., Wang, Z., Torre, R. D. L., Barling, A. N., Tsujikawa, T., Hornick, N. I., Hanifin, J. M., Simpson, E. L., Wang, Y., Swanzey, E., et al. (2016) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2016.09.020 · Cited by 28 · see citing works
“…to innate immunity by (1) restricting viral replication (Fu et al., 2015; Uchil et al., 2008), (2) inhibiting viral protein activity (Fatima et al., 2016; Fridell et al., 1995), and (3) activating innate immune signaling pathways (Albor et al., 2006; Uchil et al., 2013; Zhang et al., 2012).”
Systematic Analysis of Dimeric E3-RING Interactions Reveals Increased Combinatorial Complexity in Human Ubiquitination Networks
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Cloning and Characterization of a Gene (RFN22) Encoding a Novel Brain Expressed Ring Finger Protein (BERP) That Maps to Human Chromosome 11p15.5
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Functional Interaction between the HIV Transactivator Tat and the Transcriptional Coactivator PC4 in T Cells
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Role of Divalent Cations in HIV-1 Replication and Pathogenicity
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Different subcellular localisations of TRIM22 suggest species-specific function
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“2006) and TRIM32 interacts with tat proteins of HIV-1 and HIV-2 (Fridell et al. 1995).”
Background
NUCKS1, a novel Tat coactivator, plays a crucial role in HIV-1 replication by increasing Tat-mediated viral transcription on the HIV-1 LTR promoter
Kim, H., Choi, B., Kim, S. S., Roh, T., Park, J., & Yoon, C. (2014) · Retrovirology · doi:10.1186/s12977-014-0067-y · Cited by 23 · see citing works
“Although it has also been reported that Tat activity is modulated by Tat-interacting proteins such as Tip60, HT2A, CA150, TFIID, Tat-SF1, Tip30, p300, CREB-binding protein, PC4, and Tip110, which regulate Tat activity by regulating its interactions with TAR RNA and/or other host factors [10-20], the precise mechanisms…”
Background
Overexpression of E3 ubiquitin ligase tripartite motif 32 correlates with a poor prognosis in patients with gastric cancer
Ito, M., Migita, K., Matsumoto, S., Wakatsuki, K., Tanaka, T., Kunishige, T., Nakade, H., Nakatani, M., & Nakajima, Y. (2017) · Oncology Letters · doi:10.3892/ol.2017.5806 · Cited by 24 · see citing works
TRIM62-mediated restriction of avian leukosis virus subgroup J replication is dependent on the SPRY domain
Li, L., Feng, W., Cheng, Z., et al. (2019) · Poultry Science · doi:10.3382/ps/pez408 · Cited by 22 · see citing works
Interaction of Sp1 transcription factor with HIV‐1 Tat protein: looking for cellular partners
Loregian, A., Bortolozzo, K., Boso, S., Caputo, A., & Palù, G. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00399-5 · Cited by 22 · see citing works
Restriction factors of retroviral replication: the example of Tripartite Motif (TRIM) protein 5α and 22
Kajaste‐Rudnitski, A., Pultrone, C., Marzetta, F., Ghezzi, S., Coradin, T., & Vicenzi, E. (2009) · Amino Acids · doi:10.1007/s00726-009-0393-x · Cited by 21 · see citing works
“TRIM32 HIV-1, HIV-2 and EIAV Tat Transcription regulation Fridell et al. (1995) TRIM34 SIV CA Weak restriction activity Li et al. (2007),”
Background
The Sp1 transcription factor does not directly interact with the HIV‐1 Tat protein
Loregian, A., Bortolozzo, K., Boso, S., et al. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10271 · Cited by 21 · see citing works
“A number of cellular proteins have been reported to interact with Tat, including Tatbinding protein 1 (Nelbock et al., 1990), TBP (Kashanchi et al., 1994), TBP-associated factor TAFII55 (Chiang and Roeder, 1995), HT2A (Fridell et al., 1995), Tip60 (Kamine et al., 1996), cyclin T1 (Wei et al., 1998), Puralpha (Gallia e…”
Anti-HIV-1 activity of Trim 37
Tabah, A. A., Tardif, K. D., & Mansky, L. M. (2013) · Journal of General Virology · doi:10.1099/vir.0.057653-0 · Cited by 19 · see citing works
A Yeast TATA-Binding Protein Mutant That Selectively Enhances Gene Expression from Weak RNA Polymerase II Promoters
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“pBS/b-GAL was generated by digestion of pCMV/b-GAL (11) with EcoRI and”
MethodSelf-citation
Inhibition of the HIV Rev transactivator A new target for therapeutic intervention
Heguy, A. (1997) · Frontiers in bioscience · doi:10.2741/a191 · Cited by 19 · see citing works
“A hammerhead ribozyme targeting the common exon of the Tat and Rev genes has been shown to inhibit HIV replication in a human T cell line (84).”
BackgroundInfluential
Lentiviral Effector Pathways of TRIM Proteins
Turrini, F., Pietro, A. D., & Vicenzi, E. (2014) · DNA and Cell Biology · doi:10.1089/dna.2014.2374 · Cited by 17 · see citing works
TRIM Proteins and the Innate Immune Response to Viruses
Yap, M. W., & Stoye, J. P. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5398-7_7 · Cited by 18 · see citing works
RNAs selected in vitro by the HIV-2 tat protein
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“Candidates for cellular factors that may mediate the Tat activation domain function have been identified, including TBP [18], TAP [35], Tip60 [16], and HT2A [ 10 ].”
Background
p32 is a negative regulator of p53 tetramerization and transactivation
Ghate, N. B., Kim, J., Shin, Y., et al. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12543 · Cited by 17 · see citing works
“…protein V of adenovirus, ORF P of herpes simplex virus, EBNA-1 of Epstein–Barr virus, and HIV-1 Tat and Rev (Bruni and Roizman, 1996; Desai et al., 1991; Fridell et al., 1995; Luo et al., 1994; Matthews and Russell, 1998; Tange et al., 1996; Wang et al., 1997; Yu et al., 1995; Yu et al., 1995).”
Background
Gammaherpesvirus maintenance and replication during latency
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Tripartite Motif-Containing Protein 32 (TRIM32): What Does It Do for Skeletal Muscle?
Jeong, S. Y., Choi, J. H., Kim, J., Woo, J. S., & Lee, E. H. (2023) · Cells · doi:10.3390/cells12162104 · Cited by 14 · see citing works
“TRIM32 in skeletal muscle gained attention almost ten years after it was identified as a Tat-binding protein [2,57].”
BackgroundMethod
RING finger, B‐box, and coiled‐coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica
Miyamoto, K., Nakamura, N., Kashiwagi, M., et al. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03332.x · Cited by 15 · see citing works
Two-hybrid systems and their usage in infection biology
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Enhancement of the Basal-Level Activity of HIV-1 Long Terminal Repeat by HIV-1 Nucleocapsid Protein
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TRIM32 inhibits Venezuelan equine encephalitis virus infection by targeting a late step in viral entry
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“RING domain E3 ubiquitin ligase has been associated with the antiviral activity of the TRIM protein [20,21].”
Background
Ubiquitin ligase TRIM32 promotes dendrite arborization by mediating degradation of the epigenetic factor CDYL
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Transcriptional activation by the PHD finger is inhibited through an adjacent leucine zipper that binds 14-3-3 proteins
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trans -Dominant Mutants of E1A Provide Genetic Evidence that the Zinc Finger of the trans- Activating Domain Binds a Transcription Factor
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The maize ID1 flowering time regulator is a zinc finger protein with novel DNA binding properties
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Authors: Fridell, R. A., Harding, L. S., Bogerd, H. P., & Cullen, B. R.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Bogerd, Hal P.
Cullen, Bryan R.
Venue: Virology
Publisher: Elsevier BV
Published: 1995-06
Volume: 209
Issue: 2
Pages: 347-357
ISSN: 0042-6822 (ISSN-L)
DOI: 10.1006/viro.1995.1266
OpenAlex: W1972407993
Cited by: 129
References: 0
Citations by year: 2026: 2 · 2025: 3 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 5 · 2019: 3 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 4 · 2013: 4 · 2012: 5
FWCI: 2.35
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6621 d)
Locations: Virology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords: HIV-1 Tat protein, zinc finger proteins, transcriptional activation, protein-protein interaction, HIV-1 gene expression, nuclear protein binding
MeSH terms: Tripartite Motif Proteins, Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cell Nucleus, Chlorocebus aethiops, HeLa Cells, Humans, Kidney, Molecular Sequence Data, Recombinant Proteins, Transcription Factors, Transfection, HIV-1, HIV-2, Chloramphenicol O-Acetyltransferase, Gene Products, tat, Zinc Fingers, Sequence Homology, Amino Acid, DNA, Complementary, Ubiquitin-Protein Ligases, tat Gene Products, Human Immunodeficiency Virus

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Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins

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