The <i>fla</i> gene cluster is involved in the biogenesis of flagella in <i>Halobacterium salinarum</i>

Patenge, Nadja; Berendes, A.; Engelhardt, Harald; Schuster, Stephan C.; Oesterhelt, Dieter

doi:10.1046/j.1365-2958.2001.02542.x

Cited by 84 publications

(95 citation statements)

References 61 publications

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“…The htr15 gene is located in the archaellum operon, upstream of the flaD gene. Literature data on the whole archaellum flaDEFGHIJK gene cluster indicates that the transcript starting from htr15 locus covers the downstream gene flaD but not from flaE on [50]. The algorithmic TIS selection always chooses the first ATG or GTG but individual inspection for this case shows a putative ribosome binding site downstream of the automatically chosen TIS, located 17 nt upstream of the second potential start codon: GTGC(…)G AGGAG A T CGCGACCTCCGTGGAC(…).…”

Section: Resultsmentioning

confidence: 99%

Internal RNAs overlapping coding sequences can drive the production of alternative proteins in archaea

et al. 2018

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Prokaryotic genomes show a high level of information compaction often with different molecules transcribed from the same locus. Although antisense RNAs have been relatively well studied, RNAs in the same strand, internal RNAs (intraRNAs), are still poorly understood. The question of how common is the translation of overlapping reading frames remains open. We address this question in the model archaeon Halobacterium salinarum. In the present work we used differential RNA-seq (dRNA-seq) in H. salinarum NRC-1 to locate intraRNA signals in subsets of internal transcription start sites (iTSS) and establish the open reading frames associated to them (intraORFs). Using C-terminally flagged proteins, we experimentally observed isoforms accurately predicted by intraRNA translation for kef1, acs3 and orc4 genes. We also recovered from the literature and mass spectrometry databases several instances of protein isoforms consistent with intraRNA translation such as the gas vesicle protein gene gvpC1. We found evidence for intraRNAs in horizontally transferred genes such as the chaperone dnaK and the aerobic respiration related cydA in both H. salinarum and Escherichia coli. Also, intraRNA translation evidence in H. salinarum, E. coli and yeast of a universal elongation factor (aEF-2, fusA and eEF-2) suggests that this is an ancient phenomenon present in all domains of life.

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Section: Resultsmentioning

confidence: 99%

Internal RNAs overlapping coding sequences can drive the production of alternative proteins in archaea

et al. 2018

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“…Moreover, flagellar assembly involves homologs of components involved in the biosynthesis of bacterial type IV pili, including FlaI, an ATPase homologous to PilB, and FlaJ, a multispanning membrane protein that may provide a platform for flagellar assembly, similar to the proposed role for PilC in pilus assembly (38,44,53,54). These genes, as well as a number of others that encode proteins often required for either flagellar assembly or function (flaCDEFG and flaH), are frequently coregulated with the flg genes (11,26,44,54).…”

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Haloferax volcanii Flagella Are Required for Motility but Are Not Involved in PibD-Dependent Surface Adhesion

2010

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Although the genome of Haloferax volcanii contains genes (flgA1-flgA2) that encode flagellins and others that encode proteins involved in flagellar assembly, previous reports have concluded that H. volcanii is nonmotile. Contrary to these reports, we have now identified conditions under which H. volcanii is motile. Moreover, we have determined that an H. volcanii deletion mutant lacking flagellin genes is not motile. However, unlike flagella characterized in other prokaryotes, including other archaea, the H. volcanii flagella do not appear to play a significant role in surface adhesion. While flagella often play similar functional roles in bacteria and archaea, the processes involved in the biosynthesis of archaeal flagella do not resemble those involved in assembling bacterial flagella but, instead, are similar to those involved in producing bacterial type IV pili. Consistent with this observation, we have determined that, in addition to disrupting preflagellin processing, deleting pibD, which encodes the preflagellin peptidase, prevents the maturation of other H. volcanii type IV pilin-like proteins. Moreover, in addition to abolishing swimming motility, and unlike the flgA1-flgA2 deletion, deleting pibD eliminates the ability of H. volcanii to adhere to a glass surface, indicating that a nonflagellar type IV pilus-like structure plays a critical role in H. volcanii surface adhesion.To escape toxic conditions or to acquire new sources of nutrients, prokaryotes often depend on some form of motility. Swimming motility, a common means by which many bacteria move from one place to another, usually depends on flagellar rotation to propel cells through liquid medium (24,26,34). These motility structures are also critical for the effective attachment of bacteria to surfaces.As in bacteria, rotating flagella are responsible for swimming motility in archaea, and recent studies suggest that archaea, like bacteria, also require flagella for efficient surface attachment (37, 58). However, in contrast to bacterial flagellar subunits, which are translocated via a specialized type III secretion apparatus, archaeal flagellin secretion and flagellum assembly resemble the processes used to translocate and assemble the subunits of bacterial type IV pili (34,38,54).

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“…The estimated lengths of the mRNAs indicate that the flagellin genes within each locus are cotranscribed, but the transcripts did not include the accessory genes as seen in M. voltae and other methanogens (10,38). It was recently determined that the majority of the accessory genes observed in M. voltae are present in H. salinarum next to the flgB locus but are transcribed from a distinct promoter and in the opposite direction (29). Mutant studies with H. salinarum have shown that both loci are required for fully motile cells and that the A flagellins compose the majority of the filament, while the B flagellins make up the cell-proximal portion of the filament (36).…”

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Identification and Localization of Flagellins FlaA and FlaB3 within Flagella ofMethanococcus voltae

Bardy

Mori

Komoriya³

et al. 2002

J Bacteriol

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While they are functionally similar, archaeal flagella have characteristics not typically seen in bacterial flagella (37). Archaeal flagellins are synthesized with a leader peptide (3, 18), which is cleaved prior to the incorporation of the flagellin into the filament, similar to the processing of type IV pilins before incorporation into the pilus (34). A Methanococcus maripaludis protein (FlaK) possessing preflagellin peptidase activity has recently been reported (2). Archaeal flagellins show sequence similarity to type IV pilins at the N termini of the mature proteins (8) and do not demonstrate homology to bacterial flagellins. Archaeal flagella are thinner in diameter (10 to 13 nm [4,16,33]) than bacterial flagella (20 nm [17]) and are always composed of multiple flagellins, which are often glycosylated (6,20,24). Additionally, a search of completely sequenced archaeal genomes failed to identify genes homologous to any genes coding for structural proteins involved in bacterial flagellation (7). This includes, but is not limited to, genes encoding the hook, rod, or ring proteins. All of these characteristics suggest that the structural components of the archaeal flagella are composed of unique, archaeon-specific proteins, possibly fulfilling the same function as those present in bacterial flagella, and that the mode of assembly is likely distinct as well.Methanococcus voltae is a marine organism possessing more than 70 flagella on the cell surface. As is typical of archaeal flagella, M. voltae flagella are composed of multiple flagellins (18). There are four flagellin genes found within two transcriptional units in the M. voltae chromosome, with the first transcriptional unit containing a single flagellin gene, flaA. The second transcriptional unit includes the three remaining flagellin genes (flaB1, flaB2, and flaB3) and the downstream cotranscribed flagellar accessory genes flaCDEFGHIJ (18; N. A. Thomas and K. F. Jarrell, unpublished data). Purified flagella were shown to be composed of two major proteins, flagellins FlaB1 and FlaB2, with molecular masses corresponding to 33 and 31 kDa, respectively (18). Prior to the work presented in this study, the remaining two flagellins (FlaA and FlaB3) remained undetected.Within the flagellated archaea, little work has been done to address the universal presence of multiple flagellins. In Halobacterium salinarum, five flagellin genes are arranged in two different loci. Two flagellin genes (flgA1 and flgA2) are arranged in tandem at one locus, with the remaining three genes (flgB1, flgB2, and flgB3) clustered in another locus, and all five corresponding gene products have been identified within isolated flagella (9). The estimated lengths of the mRNAs indicate that the flagellin genes within each locus are cotranscribed, but the transcripts did not include the accessory genes as seen in M. voltae and other methanogens (10, 38). It was recently determined that the majority of the accessory genes observed in M. voltae are present in H. salinarum next to the flgB locus bu...

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The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum

Abstract: SummaryIn this study, a flagella-related protein gene cluster is described for Halobacterium salinarum. The fla gene cluster is located upstream of the flagellin genes flgB1 -3 and oriented in the opposite direction. It consists of nine open reading frames (ORFs

Cited by 84 publications

References 61 publications

Internal RNAs overlapping coding sequences can drive the production of alternative proteins in archaea

Internal RNAs overlapping coding sequences can drive the production of alternative proteins in archaea

Haloferax volcanii Flagella Are Required for Motility but Are Not Involved in PibD-Dependent Surface Adhesion

Identification and Localization of Flagellins FlaA and FlaB3 within Flagella ofMethanococcus voltae

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