A Rhomboid Protease Gene Deletion Affects a Novel Oligosaccharide N-Linked to the S-layer Glycoprotein of Haloferax volcanii

Parente, Juliana Elena; Casabuono, Adriana C.; Ferrari, María Celeste; Paggi, Roberto A.; Castro, Rosana Esther de; Couto, Alicia S.; Giménez, María Inés

doi:10.1074/jbc.m113.546531

Cited by 29 publications

(49 citation statements)

References 45 publications

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“…; Parente et al. ). In contrast, more than 30 glycosylation sites could be detected within the amino acid sequence of the S ‐layer glycoprotein from the thermophilic S. acidocaldarius and other species from the Sulfolobales .…”

Section: Discussionmentioning

confidence: 98%

“…In the mesophilic and halophilic archaeon Hfx. volcanii, seven glycosylation sites are predicted within the S-layer amino acid sequence (Jarrell et al 2010), of these six sites have been experimentally shown to be modified N-glycans (Sumper et al 1990;Mengele and Sumper 1992;Abu-Qarn et al 2007;Magidovich et al 2010;Parente et al 2014). In contrast, more than 30 glycosylation sites could be detected within the amino acid sequence of the S-layer glycoprotein from the thermophilic S. acidocaldarius and other species from the Sulfolobales.…”

Section: Discussionmentioning

confidence: 99%

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AglB, catalyzing the oligosaccharyl transferase step of the archaeal N‐glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Meyer

Albers

2014

MicrobiologyOpen

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Sulfolobus acidocaldarius, a thermo-acidophilic crenarchaeon which grows optimally at 76°C and pH 3, exhibits an astonishing high number of N-glycans linked to the surface (S-) layer proteins. The S-layer proteins as well as other surface-exposed proteins are modified via N-glycosylation, in which the oligosaccharyl transferase AglB catalyzes the final step of the transfer of the glycan tree to the nascent protein. In this study, we demonstrated that AglB is essential for the viability of S. acidocaldarius. Different deletion approaches, that is, markerless in-frame deletion as well as a marker insertion were unsuccessful to create an aglB deletion mutant. Only the integration of a second aglB gene copy allowed the successful deletion of the original aglB.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

AglB, catalyzing the oligosaccharyl transferase step of the archaeal N‐glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Meyer

Albers

2014

MicrobiologyOpen

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“…In the Gram‐negative eubacterium Providencia stuartii , the rhomboid protease AarA is required to process a pro‐form of TatA, a component of the twin‐arginine translocase secretion apparatus (Stevenson et al , ), but this function does not seem to be widely conserved because most bacteria encode a mature form of TatA. In the archaebacterium Haloferax volcanii , a rhomboid protease is involved in protein glycosylation of the S‐layer (Parente et al , ; Costa et al , ), but the molecular mechanism has not been uncovered yet. Similarly, the main model rhomboid protease GlpG of Escherichia coli , widely distributed in Gram‐negative bacteria, is extremely well‐characterised structurally and mechanistically (Strisovsky et al , ; Baker & Urban, ; Zoll et al , ), yet its biological function is unknown.…”

Section: Introductionmentioning

confidence: 99%

Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

et al. 2020

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Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive. Using proteomics, we find that Bacillus subtilis rhomboid protease YqgP interacts with the membrane-bound ATP-dependent processive metalloprotease FtsH and cleaves MgtE, the major highaffinity magnesium transporter in B. subtilis. MgtE cleavage by YqgP is potentiated in conditions of low magnesium and high manganese or zinc, thereby protecting B. subtilis from Mn 2+ /Zn 2+ toxicity. The N-terminal cytosolic domain of YqgP binds Mn 2+ and Zn 2+ ions and facilitates MgtE cleavage. Independently of its intrinsic protease activity, YqgP acts as a substrate adaptor for FtsH, a function that is necessary for degradation of MgtE. YqgP thus unites protease and pseudoprotease function, hinting at the evolutionary origin of rhomboid pseudoproteases such as Derlins that are intimately involved in eukaryotic ER-associated degradation (ERAD). Conceptually, the YqgP-FtsH system we describe here is analogous to a primordial form of "ERAD" in bacteria and exemplifies an ancestral function of rhomboid-superfamily proteins.

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“…Interestingly, rhomboid‐mediated degradation also shows conservation from a physiological point of view, as regulation of energy metabolism is a feature observed in both Shigella (Liu et al , ) and mitochondria (Spinazzi et al , ). To some extent, even the tuning of glycosylation by RHBDL4 in the ER (Knopf et al , ) may be functionally paralleled by an archaeal rhomboid protease, Haloferax volcanii RhoII (Parente et al , ).…”

Section: Rhomboid Proteases and Pseudoproteases Target Proteins For Dmentioning

confidence: 99%

Derlins with scissors: primordial ERAD in bacteria

Knopf

Lemberg

2020

The EMBO Journal

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Rhomboid intramembrane serine proteases are present in all kingdoms of life, but as we do not know their substrates in many species, it remains puzzling why rhomboids are among the most‐conserved integral membrane proteins. Two new studies in The EMBO Journal by Began et al and Liu et al now link bacterial rhomboid proteases to membrane protein degradation, showing striking similarities to what is known about eukaryotic rhomboid family proteins, thus pointing toward a conserved membrane surveillance mechanism.

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A Rhomboid Protease Gene Deletion Affects a Novel Oligosaccharide N-Linked to the S-layer Glycoprotein of Haloferax volcanii

Cited by 29 publications

References 45 publications

AglB, catalyzing the oligosaccharyl transferase step of the archaeal N‐glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

AglB, catalyzing the oligosaccharyl transferase step of the archaeal N‐glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

Derlins with scissors: primordial ERAD in bacteria

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