The AAA team: related ATPases with diverse functions

Latterich, Martin; Patel, Sheetal

doi:10.1016/s0962-8924(98)80014-7

Cited by 164 publications

(13 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Finally, for the T6SS a AAA ATPase, called ClpV1, ClpV2, or ClpV3 in P. aeruginosa , is involved. The AAA motif is a conserved sequence of about 250 residues that includes the Walker sequences and other domains unique to AAA proteins (Patel and Latterich, 1998). It is remarkable that each secretion system described previously involves an ATPase of a distinct family.…”

Section: Molecular Needs For the Function Of Secretion Machinesmentioning

confidence: 99%

Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function

Filloux¹

2011

Front. Microbio.

153

179

View full text Add to dashboard Cite

Protein secretion systems are molecular nanomachines used by Gram-negative bacteria to thrive within their environment. They are used to release enzymes that hydrolyze complex carbon sources into usable compounds, or to release proteins that capture essential ions such as iron. They are also used to colonize and survive within eukaryotic hosts, causing acute or chronic infections, subverting the host cell response and escaping the immune system. In this article, the opportunistic human pathogen Pseudomonas aeruginosa is used as a model to review the diversity of secretion systems that bacteria have evolved to achieve these goals. This diversity may result from a progressive transformation of cell envelope complexes that initially may not have been dedicated to secretion. The striking similarities between secretion systems and type IV pili, flagella, bacteriophage tail, or efflux pumps is a nice illustration of this evolution. Differences are also needed since various secretion configurations call for diversity. For example, some proteins are released in the extracellular medium while others are directly injected into the cytosol of eukaryotic cells. Some proteins are folded before being released and transit into the periplasm. Other proteins cross the whole cell envelope at once in an unfolded state. However, the secretion system requires conserved basic elements or features. For example, there is a need for an energy source or for an outer membrane channel. The structure of this review is thus quite unconventional. Instead of listing secretion types one after each other, it presents a melting pot of concepts indicating that secretion types are in constant evolution and use basic principles. In other words, emergence of new secretion systems could be predicted the way Mendeleïev had anticipated characteristics of yet unknown elements.

show abstract

Section: Molecular Needs For the Function Of Secretion Machinesmentioning

confidence: 99%

Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function

Filloux¹

2011

Front. Microbio.

153

179

View full text Add to dashboard Cite

show abstract

“…The AAA family includes regulatory components of proteases, proteasomal subunits, peroxisomal biogenesis proteins, Mg 2+ and CO 2+ chelatases, vesicle synthesis protein, dynein motor protein, and proteins involved in DNA replication, recombination, restriction, and transcription as well as sporulation in bacteria (Patel and Latterich, 1998;Neuwald et al, 1999). Among them RuvBL1, a helicase homologous to RuvB of E. coli, plays important roles in the late stages of homologous genetic recombination and the recombinational repair of damaged DNA (Kanemaki et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Isolation of HELAD1, a novel human helicase gene up-regulated in colorectal carcinomas

et al. 2002

View full text Add to dashboard Cite

To investigate the mechanisms of colorectal carcinogenesis, we searched for genes regulated by adenomatous polyposis coli gene product (APC) and identified a novel gene, termed HELAD1 (helicase, APC down-regulated 1). A recombinant polypeptide representing the ATPases associated with cellular activities (AAA) domain of the HELAD1 product showed 3' to 5' helicase activity and exonuclease activity in vitro. HELAD1 was abundantly expressed in 16 of 20 colon cancers examined but hardly detectable in corresponding non-cancerous mucosae. Treatment of colon-cancer cells with antisense oligonucleotides suppressed its expression and induced apoptosis. These data revealed an importance of HELAD1 in colorectal carcinogenesis and suggest that suppression of HELAD1 may be a promising therapeutic strategy.

show abstract

“…Immediately after the motif B is the second region of homology (SRH) which is also known as the "AAA minimum consensus" (Latterich & Patel, 1998;Tomoyasu et al, 1993). This region together with the Walker motifs was originally used to define the members of the classical AAA family.…”

Section: Resultsmentioning

confidence: 99%

“…(AAA proteins) where the members share a conserved ATP-binding domain called the AAA domain (Confalonieri & Duguet, 1995;Latterich & Patel, 1998). However, information garnered from various bioinformatics analyses and structural studies (e.g.…”

Section: Conservation Of the Domains Predicted By Smart In Other Py23mentioning

confidence: 99%

Novel insights into the biological function of the high molecular weight PY235 rhoptry protein of plasmodium Yoelii

Ramalingam¹

View full text Add to dashboard Cite

show abstract

The AAA team: related ATPases with diverse functions

Cited by 164 publications

References 54 publications

Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function

Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function

Isolation of HELAD1, a novel human helicase gene up-regulated in colorectal carcinomas

Novel insights into the biological function of the high molecular weight PY235 rhoptry protein of plasmodium Yoelii

Contact Info

Product

Resources

About