Human t-Complex Protein 11 (TCP11), a Testis-Specific Gene Product, Is a Potential Determinant of the Sperm Morphology

Abstract The t-complex is defined as naturally occurring variants of the proximal third of mouse chromosome 17 and has been studied by mouse geneticists for decades. This region contains many genes involved in processes from embryogenesis to sperm function. One such gene, t-complex protein 11 (Tcp11), was identified as a testis-specific gene whose protein is present in elongating spermatids. Later work on Tcp11 localized TCP11 to the sperm surface and acrosome cap and implicated TCP11 as important for sperm capacitation through the cyclic AMP/Protein Kinase A pathway. Here, we show that TCP11 is cytoplasmically localized to elongating spermatids and absent from sperm. In the absence of Tcp11, male mice have severely reduced fertility due to a significant decrease in progressively motile sperm; however, Tcp11-null sperm continues to undergo tyrosine phosphorylation, a hallmark of capacitation. Interestingly, null sperm displays reduced PKA activity, consistent with previous reports. Our work demonstrates that TCP11 functions in elongated spermatids to confer proper motility in mature sperm.

Download Full-text

Faculty Opinions recommendation of Characterisation of the gene encoding a protective antigen from Babesia microti identified it as eta subunit of chaperonin containing T-complex protein 1.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1002445.27154 ◽

2001 ◽

Author(s):

David Persing

Keyword(s):

Protective Antigen ◽

Babesia Microti ◽

Gene Encoding ◽

T Complex ◽

Complex Protein

Download Full-text

Yeast repressor alpha 2 binds to its operator cooperatively with yeast protein Mcm1.

Molecular and Cellular Biology ◽

10.1128/mcb.9.11.5228 ◽

1989 ◽

Vol 9 (11) ◽

pp. 5228-5230 ◽

Cited By ~ 54

Author(s):

C A Keleher ◽

S Passmore ◽

A D Johnson

Keyword(s):

Saccharomyces Cerevisiae ◽

Gene Product ◽

Strong Evidence ◽

Regulatory Proteins ◽

Yeast Cells ◽

Specific Gene ◽

Yeast Gene ◽

Yeast Protein ◽

Transcriptional Regulatory

To bring about repression of a family fo genes in Saccharomyces cerevisiae called the a-specific genes, two transcriptional regulatory proteins, alpha 2 and GRM (general regulator of matin type), bind cooperatively to an operator found upstream of each a-specific gene. To date, GRM has been defined only biochemically. In this communication we show that the product of a single yeast gene (MCM1) is sufficient to bind cooperatively with alpha 2 to the operator. We also show that antiserum raised against the MCM1 gene product recognizes GRM from yeast cells. These results, in combination with previous observations, provide strong evidence that MCM1 encodes the GRM activity.

Download Full-text

Polycomb Requires Chaperonin Containing TCP-1 Subunit 7 for Maintaining Gene Silencing in Drosophila

Frontiers in Cell and Developmental Biology ◽

10.3389/fcell.2021.727972 ◽

2021 ◽

Vol 9 ◽

Author(s):

Najma Shaheen ◽

Jawad Akhtar ◽

Zain Umer ◽

Muhammad Haider Farooq Khan ◽

Mahnoor Hussain Bakhtiari ◽

...

Keyword(s):

Genetic Interaction ◽

Expression Patterns ◽

Cell Types ◽

Polycomb Group ◽

Specific Gene ◽

Cellular Memory ◽

Trithorax Group ◽

T Complex ◽

Ring Complex ◽

Active Expression

In metazoans, heritable states of cell type-specific gene expression patterns linked with specialization of various cell types constitute transcriptional cellular memory. Evolutionarily conserved Polycomb group (PcG) and trithorax group (trxG) proteins contribute to the transcriptional cellular memory by maintaining heritable patterns of repressed and active expression states, respectively. Although chromatin structure and modifications appear to play a fundamental role in maintenance of repression by PcG, the precise targeting mechanism and the specificity factors that bind PcG complexes to defined regions in chromosomes remain elusive. Here, we report a serendipitous discovery that uncovers an interplay between Polycomb (Pc) and chaperonin containing T-complex protein 1 (TCP-1) subunit 7 (CCT7) of TCP-1 ring complex (TRiC) chaperonin in Drosophila. CCT7 interacts with Pc at chromatin to maintain repressed states of homeotic and non-homeotic targets of PcG, which supports a strong genetic interaction observed between Pc and CCT7 mutants. Depletion of CCT7 results in dissociation of Pc from chromatin and redistribution of an abundant amount of Pc in cytoplasm. We propose that CCT7 is an important modulator of Pc, which helps Pc recruitment at chromatin, and compromising CCT7 can directly influence an evolutionary conserved epigenetic network that supervises the appropriate cellular identities during development and homeostasis of an organism.

Download Full-text

CTGF/Hcs24, a hypertrophic chondrocyte-specific gene product, stimulates proliferation and differentiation, but not hypertrophy of cultured articular chondrocytes

Journal of Cellular Physiology ◽

10.1002/jcp.10113 ◽

2002 ◽

Vol 192 (1) ◽

pp. 55-63 ◽

Cited By ~ 84

Author(s):

Takashi Nishida ◽

Satoshi Kubota ◽

Tohru Nakanishi ◽

Takuo Kuboki ◽

Gen Yosimichi ◽

...

Keyword(s):

Gene Product ◽

Articular Chondrocytes ◽

Specific Gene ◽

Hypertrophic Chondrocyte ◽

Proliferation And Differentiation

Download Full-text

TCP1γ Subunit Is Indispensable for Growth and Infectivity of Leishmania donovani

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.00669-20 ◽

2020 ◽

Vol 64 (8) ◽

Cited By ~ 1

Author(s):

Shailendra Yadav ◽

Jitendra Kuldeep ◽

Mohammad I. Siddiqi ◽

Neena Goyal

Keyword(s):

Cell Cycle Progression ◽

Leishmania Donovani ◽

Gene Replacement ◽

Titration Calorimetry ◽

Content Type ◽

T Complex ◽

Complex Protein ◽

Oligomeric Complex

ABSTRACT T-complex protein-1 (TCP1) is a ubiquitous group II chaperonin and is known to fold various proteins, such as actin and tubulin. In Leishmania donovani, the γ subunit of TCP1 (LdTCP1γ) has been cloned and characterized. It forms a high-molecular-weight homo-oligomeric complex that performs ATP-dependent protein folding. In the present study, we evaluated the essentiality of the LdTCP1γ gene. Gene replacement studies indicated that LdTCP1γ is essential for parasite survival. The LdTCP1γ single-allele-replacement mutants exhibited slowed growth and decreased infectivity in mouse macrophages compared to the growth and infectivity of the wild-type parasites. Modulation of LdTCP1γ expression in promastigotes also modulated cell cycle progression. Suramin, an antitrypanosomal drug, not only inhibited the luciferase refolding activity of the recombinant LdTCP1γ (rLdTCP1γ) homo-oligomeric complex but also exhibited potential antileishmanial efficacy both in vitro and in vivo. The interaction of suramin and LdTCP1γ was further validated by isothermal titration calorimetry. The study suggests LdTCP1γ as a potential drug target and also provides a framework for the development of a new class of drugs.

Download Full-text